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protein detection techniques can be used to find disease biomarkers like specific proteins or antibodies. It is thought to be a viable method for identifying particular proteins during the diagnosis of diseases like cancer, autoimmune disease, and prion disorders. The detection of several biomarkers used in the diagnosis of neurological and oncological illnesses by
Western blotting is a common procedure. For instance, it is widely believed that the advent of multidrug resistance (MDR) has made effective cancer therapy extremely challenging. Therefore, early, accurate, and sensitive MDR mechanism discovery is essential, as is the search for more effective chemotherapeutic approaches for application in clinical settings. The expression of MDR1/P-glycoprotein in the P388/ADR, P388 and HCT-15 cell lines is examined using the WB technique. WB has also identified MRP1 levels.
288:
Creutzfeldt-Jakob disease. Also, Farmers lung disease is a pulmonary condition brought on by breathing antigenic particles, and studies have indicated that western blot may be a useful option for identifying immunoreactive proteins related to farmers lung disease. Besides, western blot is also used to identify proteins in synovial fluid and serum, enabling the diagnosis of osteoarthritis and rheumatoid arthritis clinical symptoms. western blot is used to assess the levels of FSTL1 protein expression in individuals with knee osteoarthritis, which serves as a potential biomarker of articular damage. Additionally, it is used to identify proteins in
900:. The isoelectric point of a given protein is determined by the relative number of positively (e.g. lysine, arginine) and negatively (e.g. glutamate, aspartate) charged amino acids, with negatively charged amino acids contributing to a low isoelectric point and positively charged amino acids contributing to a high isoelectric point. Samples could also be separated first under nonreducing conditions using SDS-PAGE, and under reducing conditions in the second dimension, which breaks apart disulfide bonds that hold subunits together. SDS-PAGE might also be coupled with urea-PAGE for a 2-dimensional gel.
611:. Although non-fat dry milk is preferred due to its availability, an appropriate blocking solution is needed as not all proteins in milk are compatible with all the detection bands. The protein in the dilute solution attaches to the membrane in all places where the target proteins have not attached. Thus, when the antibody is added, it cannot bind to the membrane, and therefore the only available binding site is the specific target protein. This reduces background in the final product of the western blot, leading to clearer results, and eliminates false positives.
750:
320:
174:
302:
function and localization suggests that when proteins move, their functions may change or acquire new characteristics. A protein's subcellular placement can be determined using a variety of methods. Numerous efficient and reliable computational tools and strategies have been created and used to identify protein subcellular localization. With the aid of subcellular fractionation methods, WB continues to be an important fundamental method for the investigation and comprehension of protein localization.
384:
homogenization method needs to be chosen due to the fact that it is responsible for bursting the cell membrane and releasing the intracellular components. Besides that, the ideal lysis buffer is needed to acquire substantial amounts of target protein content because the buffer is leading the process of protein solubilization and preventing protein degradation. After completing the sample preparation, the protein content is ready to be separated by the utilization of gel electrophoresis.
961:
antibodies since the quality of the antibodies plays a significant role in the detection of proteins specifically. On account of the presence of these kinds of problems, a variety of improvements are being produced in the fields of preparation of cell lysate and blotting procedures to build up reliable results. Moreover, to achieve more sensitive analysis and overcome the problems associated with western blotting, several different techniques have been developed and utilized, such as
399:
532:. Electroblotting uses an electric current to pull the negatively charged proteins from the gel towards the positively charged anode, and into the PVDF or NC membrane. The proteins move from within the gel onto the membrane while maintaining the organization they had within the gel. An older method of transfer involves placing a membrane on top of the gel, and a stack of filter papers on top of that. The entire stack is placed in a buffer solution which moves up the paper by
1118:
311:
mapping." Finding the binding epitope of an antibody is essential for the discovery and creation of novel vaccines, diagnostics, and therapeutics. As a result, various methods for mapping antibody epitopes have been created. At this point, western blotting's specificity is the main feature that sets it apart from other epitope mapping techniques. There are several application of western blot for epitope mapping on human skin samples, hemorrhagic disease virus.
20:
510:
549:
833:
1104:
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photopatternable (blue-light) surface are the foundation of this multistep procedure. Due to improvements in analytical performance, WB may now be completed in 10–60 minutes while maintaining high sensitivity detection limits (50 picomoles) and multiplexed component detection levels (femtograms). Therefore, by fusing superb specificity and the high-throughput benefits of multiplexing, WB creates a cornerstone for quick proteomics.
620:
694:. Therefore, the production of luminescence is proportional to the amount of horseradish peroxidase-conjugated secondary antibody, and therefore, indirectly measures the presence of the target protein. A sensitive sheet of photographic film is placed against the membrane, and exposure to the light from the reaction creates an image of the antibodies bound to the blot. A cheaper but less sensitive approach utilizes a
877:
block conditions, the concentration of antibodies, and identification and quantitative determination methods. Many of the articles that have been published don't cover all of these variables. Hence, it is crucial to describe different experimental circumstances or parameters in order to increase the repeatability and precision of WB. To increase WB repeatability, a minimum reporting criteria is thus required.
737:
detection process. Given the advent of high-throughput protein analysis and lower limits of detection, however, there has been interest in developing one-step probing systems that would allow the process to occur faster and with fewer consumables. This requires a probe antibody which both recognizes the protein of interest and contains a detectable label, probes which are often available for known
224:-infected cells are separated and blotted on a membrane as above. Then, the serum to be tested is applied in the primary antibody incubation step; free antibody is washed away, and a secondary anti-human antibody linked to an enzyme signal is added. The stained bands then indicate the proteins to which the patient's serum contains antibody. A western blot is also used as the definitive test for
280:. Recent research utilizing the western blot technique showed an improved detection of EPO in blood and urine based on novel Velum SAR precast horizontal gels optimized for routine analysis. With the adoption of the horizontal SAR-PAGE in combination with the precast film-supported Velum SAR gels the discriminatory capacity of micro-dose application of rEPO was significantly enhanced.
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weight region because some proteins form dimers, trimers, and multimers; this issue might be solved by heating the sample for longer periods of time. Proteins with post-translational modifications (PTMs) or numerous isoforms cause several bands to appear at various molecular weight areas. PTMs can be removed from a specimen using specific chemicals, which also remove extra bands.
193:). At least 8–9% of all protein-related publications are estimated to apply western blots. It is used as a general method to identify the presence of a specific single protein within a complex mixture of proteins. A semi-quantitative estimation of a protein can be derived from the size and colour intensity of a protein band on the blot membrane. In addition, applying a
1024:
aid of single-cell WB, the western blot's selectivity and specificity were expanded to include single-cell protein analysis. The limitations of antibody accuracy and sensitivity are overcome by this technique. Furthermore, because of its versatility, it may be utilized to measure numerous target proteins concurrently from different cell lines and single cells.
453:). The concentration of acrylamide determines the resolution of the gel – the greater the acrylamide concentration, the better the resolution of lower molecular weight proteins. The lower the acrylamide concentration, the better the resolution of higher molecular weight proteins. Proteins travel only in one dimension along the gel for most blots.
357:(as well as in the gel) in order to give all proteins present a uniform negative charge, since proteins can be positively, negatively, or neutrally charged. Prior to electrophoresis, protein samples are often boiled to denature the proteins present. This ensures that proteins are separated based on size and prevents
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Balakrishnan, Lavanya; Bhattacharjee, Mitali; Ahmad, Sartaj; Nirujogi, Raja Sekhar; Renuse, Santosh; Subbannayya, Yashwanth; Marimuthu, Arivusudar; Srikanth, Srinivas M; Raju, Rajesh; Dhillon, Mukesh; Kaur, Navjyot; Jois, Ramesh; Vasudev, Vivek; Ramachandra, YL; Sahasrabuddhe, Nandini A (2014-01-06).
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It is a technique that combines conventional SDS-PAGE protein resolution with a bead-based microarray platform that immobilizes proteins on microspheres. This combination of protein separation, uniformity, and sensitivity allows for the quick quantification of a number of different protein targets as
814:
which capture a digital image of the western blot or photographic film. The use of film for western blot detection is slowly disappearing because of non linearity of the image (non accurate quantification). The image is analysed by densitometry, which evaluates the relative amount of protein staining
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positioned beneath the nitrocellulose membrane while the proteins are kept in the membrane. Then, specific antibodies are used to identify the proteins, and a radioactive label is used to identify the DNA. Furthermore, the transmitted proteins and DNA can be retrieved and examined in greater detail.
951:
It has been claimed that a variety of odd and unequal bands, including black dots, white spots or bands, and curving bands, have occurred. The block dots are removed from the blots by effective blocking. White patches develop as a result of bubbles between the membrane and gel. White bands appear in
924:
There may be a weak or absent signal in the band for a number of reasons related to the amount of antibody and antigen used. This problem might be resolved by using the ideal antigen and antibody concentrations and dilutions specified in the supplier's data sheet. Increasing the exposition period in
876:
In order to ensure that the results of
Western blots are reproducible, it is important to report the various parameters mentioned above, including specimen preparation, the concentration of protein used for loading, the percentage of gel and running condition, various transfer methods, attempting to
867:
One major difference between nitrocellulose and PVDF membranes relates to the ability of each to support "stripping" antibodies off and reusing the membrane for subsequent antibody probes. While there are well-established protocols available for stripping nitrocellulose membranes, the sturdier PVDF
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cultures). The secondary antibody recognises and binds to the species-specific portion of the primary antibody. Therefore, an anti-mouse secondary antibody will bind to almost any mouse-sourced primary antibody, and can be referred to as an 'anti-species' antibody (e.g. anti-mouse, anti-goat etc.).
727:
Protein A or
Streptavidin with a radioactive isotope of iodine. Since other methods are safer, quicker, and cheaper, this method is now rarely used; however, an advantage of this approach is the sensitivity of auto-radiography-based imaging, which enables highly accurate protein quantification when
717:
Another method of secondary antibody detection utilizes a near-infrared fluorophore-linked antibody. The light produced from the excitation of a fluorescent dye is static, making fluorescent detection a more precise and accurate measure of the difference in the signal produced by labeled antibodies
556:
Total protein staining allows the total protein that has been successfully transferred to the membrane to be visualised, allowing the user to check the uniformity of protein transfer and to perform subsequent normalization of the target protein with the actual protein amount per lane. Normalization
539:
As a result of either transfer process, the proteins are exposed on a thin membrane layer for detection. Both varieties of membrane are chosen for their non-specific protein binding properties (i.e. binds all proteins equally well). Protein binding is based upon hydrophobic interactions, as well as
287:
On the other hand, as western blot has the potential to distinguish different protein isoforms, it may be used to diagnose prion and protein isoform-related diseases, such as cancer. For instance, the western blotting analysis of the isoform pattern of 14-3-3 proteins in cerebral fluid can identify
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The capillary and microchip electrophoresis-based western blot was created to reduce the quantity of protein samples and the amount of time it takes to execute western blot. It contributes to the more sensitive and accurate measurement of various protein targets from any single-cell lysate carried
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A enhanced WB technique called multistrip WB is based on the simultaneous transfer of different proteins from a number of polyacrylamide gel strips to a single polyvinylidene difluoride or nitrocellulose membrane. Multistrip WB allows for the simultaneous monitoring of up to nine separate proteins
1041:
Quantitative computerized western blot analyses the reactivity of individual antibodies to specific antigens to identify immunodominant and immunorecessive determinants using two measures, such as net band intensity and total lane intensity of the WB. The creation of quick serodiagnostic tests and
1023:
The single-cell WB (scWB), in addition to the conventional WB, is regarded as a breakthrough in the study of protein subcellular localization and in the evaluation of single-cell protein. When measuring the levels and conditions of protein expression from one cell to the next, it is used. With the
823:
Radioactive labels do not require enzyme substrates, but rather, allow the placement of medical X-ray film directly against the western blot, which develops as it is exposed to the label and creates dark regions which correspond to the protein bands of interest (see image above). The importance of
757:
After the unbound probes are washed away, the western blot is ready for detection of the probes that are labeled and bound to the protein of interest. In practical terms, not all westerns reveal protein only at one band in a membrane. Size approximations are taken by comparing the stained bands to
627:
During the detection process, the membrane is "probed" for the protein of interest with a modified antibody which is linked to a reporter enzyme; when exposed to an appropriate substrate, this enzyme drives a colorimetric reaction and produces a colour. For a variety of reasons, this traditionally
2392:
Balakrishnan, Lavanya; Bhattacharjee, Mitali; Ahmad, Sartaj; Nirujogi, Raja Sekhar; Renuse, Santosh; Subbannayya, Yashwanth; Marimuthu, Arivusudar; Srikanth, Srinivas M; Raju, Rajesh; Dhillon, Mukesh; Kaur, Navjyot; Jois, Ramesh; Vasudev, Vivek; Ramachandra, Yl; Sahasrabuddhe, Nandini A (December
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The method with the highest adoption rate for determining DNA-binding proteins and protein-DNA interactions is the electrophoretic mobility shift test. Protein-DNA complexes are analysed via shift-WB. It is created by transferring protein-DNA complexes, in which the DNA in the charged membrane is
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When the protein is broken down by proteases, several bands other than predicted bands of low molecular weight might appear. The development of numerous bands can be prevented by properly preparing protein samples with enough protease inhibitors. Multiple bands might show up in the high molecular
794:) that is bound to the secondary antibody. This converts the soluble dye into an insoluble form of a different colour that precipitates next to the enzyme and thereby stains the membrane. Development of the blot is then stopped by washing away the soluble dye. Protein levels are evaluated through
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In addition to the application of western blot in scientific research, it is also utilized in clinical research areas. Since it can be applied to the direct protein identification process, western blot is regarded as a powerful diagnostic tool that is frequently used in the clinic setting. WB and
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and blood transfusions. Each is prohibited under WADA's List of
Prohibited Substances and Methods. The western blot technique was used during the 2014 FIFA World Cup in the anti-doping campaign for that event. In total, over 1000 samples were collected and analysed by Reichel, et al. in the WADA
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The development known as quantifiable fluorescence-based WB (QFWB) enables researchers to carry out comparative expression analysis with better sensitivity and precision than ever before. Quantifiable in QFWB refers to genuinely quantitative with increased sensitivity. This method is employed to
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Historically, the probing process was performed in two steps because of the relative ease of producing primary and secondary antibodies in separate processes. This gives researchers and corporations huge advantages in terms of flexibility, reduction of cost, and adds an amplification step to the
383:
As a significant step in conducting a western blot, sample preparation has to be done effectively since the interpretation of this assay is influenced by the protein preparation, which is composed of protein extraction and purification processes. To achieve efficient protein extraction, a proper
1005:
Since 1980, western blot has emerged as the most used method in molecular biology for determining the presence and quantity of a certain protein. Over the years, plenty of "advanced" and "optimized" systematical methods have been developed. These developments provide advanced and more sensitive
960:
During the western blotting, there could be several problems related to the different steps of this procedure. Those problems could originate from a protein analysis step such as the detection of low- or post-translationally modified proteins. Additionally, they can be based on the selection of
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allows for easier stripping, and for more reuse before background noise limits experiments. Another difference is that, unlike nitrocellulose, PVDF must be soaked in 95% ethanol, isopropanol or methanol before use. PVDF membranes also tend to be thicker and more resistant to damage during use.
858:
probe is excited by light and the emission of the excitation is then detected by a photosensor such as a CCD camera equipped with appropriate emission filters which captures a digital image of the western blot and allows further data analysis such as molecular weight analysis and a quantitative
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C. It can also be incubated at different temperatures, with lesser temperatures being associated with more binding, both specific (to the target protein, the "signal") and non-specific ("noise"). Following incubation, the membrane is washed several times in wash buffer to remove unbound primary
370:
specific to the target protein. Lastly, the membrane will be stained with a secondary antibody that recognizes the first antibody staining, which can then be used for detection by a variety of methods. The gel electrophoresis step is included in western blot analysis to resolve the issue of the
310:
Due to their various epitopes, antibodies have gained interest in both basic and clinical research. The foundation of antibody characterization and validation is epitope mapping. The procedure of identifying an antibody's binding sites (epitopes) on the target protein is referred to as "epitope
301:
For medication development, the identification of therapeutic targets, and biological research, it is essential to comprehend where proteins are located within a cell. The subcellular locations of proteins inside the cell and their functions are closely related. The relationship between protein
590:
Since the membrane has been chosen for its ability to bind protein and as both antibodies and the target are proteins, steps must be taken to prevent the interactions between the membrane and the antibody used for detection of the target protein. Blocking of non-specific binding is achieved by
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identify the minute expression variations between various samples. With the aid of a secondary antibody that has been fluorescently tagged, QFWB produces a linear detection profile. Modern QFWB techniques enable simultaneous dual labeling and are more sensitive to identify minute variations.
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In order to detect many proteins on a single microfluidic chip, microfluidic western blot is carried out using a number of processes, including sample enrichment, protein size, deposition of protein, and then in situ antibody probing. A photoreactive (UV light) polyacrylamide gel and a
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is the misuse of certain techniques and/or substances to increase one's red blood cell mass, which allows the body to transport more oxygen to muscles and therefore increase stamina and performance. There are three widely known substances or methods used for blood doping, namely,
952:
the blots when main and secondary antibodies are present in significant concentrations. Because of the high voltage used during the gel run and the rapid protein migration, smiley bands appear in the blots. The strange bands in the blot are resolved by resolving these problems.
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are generated when a host species or immune cell culture is exposed to the protein of interest (or a part thereof). Normally, this is part of the immune response, whereas here they are harvested and used as sensitive and specific detection tools that bind the protein directly.
528:). NC membrane has high affinity for protein and its retention abilities. However, NC is brittle, and does not allow the blot to be used for re-probing, whereas PVDF membrane allows the blot to be re-probed. The most commonly used method for transferring the proteins is called
718:
bound to proteins on a western blot. Proteins can be accurately quantified because the signal generated by the different amounts of proteins on the membranes is measured in a static state, as compared to chemiluminescence, in which light is measured in a dynamic state.
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well as their changes. The benefit of DigiWest is that western blot is carried out using beads-based microarrays, allowing for the simultaneous detection and analysis of hundreds of distinct proteins and their changes using a wide range of varied antibodies.
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and serum, enabling the diagnosis of osteoarthritis and rheumatoid arthritis clinical symptoms. It is used to assess the levels of FSTL1 protein expression in individuals with knee osteoarthritis, which serves as a potential biomarker of articular damage.
59:
Western blot technique uses three elements to achieve its task of separating a specific protein from a complex: separation by size, transfer of protein to a solid support, and marking target protein using a primary and secondary antibody to visualize. A
561:
of housekeeping proteins in the classical procedure, but is heading toward total protein staining recently, due to multiple benefits. At least seven different approaches for total protein staining have been described for western blot normalization:
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efficient vaccines is made possible by the identification of certain immunodominant antigens.The study looks for serological markers for the early diagnosis of cancer, viral, and autoimmune illnesses using quantitative computerized western blot.
644:
After blocking, a solution of primary antibody (generally between 0.5 and 5 micrograms/mL) diluted in either PBS or TBST wash buffer is incubated with the membrane under gentle agitation for typically an hour at room temperature, or overnight at
891:
Two-dimensional SDS-PAGE uses the principles and techniques outlined above. 2-D SDS-PAGE, as the name suggests, involves the migration of polypeptides in 2 dimensions. For example, in the first dimension, polypeptides are separated according to
161:. The Towbin group also used secondary antibodies for detection, thus resembling the actual method that is almost universally used today. Between 1979 and 2019 "it has been mentioned in the titles, abstracts, and keywords of more than 400,000
1465:
Burnette WN (April 1981). ""Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate--polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A".
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Strong antibody concentrations, inadequate blocking, inadequate washing, and excessive exposure time during imaging can result in a high background in the blots. A high background in the blots could be avoided by fixing these issues.
2108:
Sinkala, Elly; Sollier-Christen, Elodie; Renier, Corinne; RosĂ s-Canyelles, Elisabet; Che, James; Heirich, Kyra; Duncombe, Todd A.; Vlassakis, Julea; Yamauchi, Kevin A.; Huang, Haiyan; Jeffrey, Stefanie S.; Herr, Amy E. (2017-03-23).
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testing employ western blotting. A western blot can also be used as a confirmatory test for
Hepatitis B infection and HSV-2 (Herpes Type 2) infection. In veterinary medicine, a western blot is sometimes used to confirm
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from the same loading of the sample and up to a tenfold increase in data output for a single WB cycle. Systems biology, cell signaling research, and biomedical diagnostics would all benefit from using this technique.
365:
in order to visualize the proteins on the blot and ensure a proper transfer occurred. Next the proteins are blocked with milk (or other blocking agents) to prevent non-specific antibody binding, and then stained with
361:(enzymes that break down proteins) from degrading samples. Following electrophoretic separation, the proteins are transferred to a membrane (typically nitrocellulose or PVDF). The membrane is often then stained with
683:. This means that several secondary antibodies will bind to one primary antibody and enhance the signal, allowing the detection of proteins of a much lower concentration than would be visible by SDS-PAGE alone.
713:
procedures, the enzyme can be provided with a substrate molecule that will be converted by the enzyme to a coloured reaction product that will be visible on the membrane (see the figure below with blue bands).
55:
in a sample of tissue homogenate or extract. Besides detecting the proteins, this technique is also utilized to visualize, distinguish, and quantify the different proteins in a complicated protein combination.
824:
radioactive detections methods is declining due to its hazardous radiation , because it is very expensive, health and safety risks are high, and ECL (enhanced chemiluminescence) provides a useful alternative.
517:
To make the proteins accessible to antibody detection, they are moved from within the gel onto a membrane, a solid support, which is an essential part of the process. There are two types of membrane:
1934:"Herpes simplex virus type 2 (HSV-2) Western blot confirmatory testing among men testing positive for HSV-2 using the focus enzyme-linked immunosorbent assay in a sexually transmitted disease clinic"
810:
Chemiluminescent detection methods depend on incubation of the western blot with a substrate that will luminesce when exposed to the reporter on the secondary antibody. The light is then detected by
650:
antibody, and thereby minimize background. Typically, the wash buffer solution is composed of buffered saline solution with a small percentage of detergent, and sometimes with powdered milk or BSA.
907:
of a particular protein – e.g. a protein that has been phosphorylated (by addition of a negatively charged group). Proteins that have been separated can be cut out of the gel and then analysed by
741:. The primary probe is incubated with the membrane in a manner similar to that for the primary antibody in a two-step process, and then is ready for direct detection after a series of wash steps.
425:
gels and buffers loaded with sodium dodecyl sulfate (SDS). SDS-PAGE (SDS-polyacrylamide gel electrophoresis) maintains polypeptides in a denatured state once they have been treated with strong
903:
In principle, this method allows for the separation of all cellular proteins on a single large gel. A major advantage of this method is that it often distinguishes between different
582:. In order to avoid noise of signal, total protein staining should be performed before blocking of the membrane. Nevertheless, post-antibody stainings have been described as well.
1896:"Western blot analysis of the reactivity between envelope proteins of hepatitis B viruses from Brazilian carriers and antibodies raised against recombinant hepatitis B vaccines"
197:
of a purified protein of known concentrations can be used to allow a more precise estimate of protein concentration. The western blot is routinely used for verification of
2174:
Bouillet, L; Baudet, A E; Deroux, A; Sidibé, A; Dumestre-Perard, C; Mannic, T; Treillard, B; Arboleas, M A; Chiquet, C A; Gulino-Debrac, D G; Vilgrain, I Y (2013-11-01).
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and quantifies the results in terms of optical density. Newer software allows further data analysis such as molecular weight analysis if appropriate standards are used.
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charged interactions between the membrane and protein. Nitrocellulose membranes are cheaper than PVDF, but are far more fragile and cannot withstand repeated probings.
346:
273:
141:. The term "western blot" was given by W. Neal Burnette in 1981, although the method itself was independently invented in 1979 by Jaime Renart, Jakob Reiser, and
2091:
721:
A third alternative is to use a radioactive label rather than an enzyme coupled to the secondary antibody, such as labeling an antibody-binding protein like
702:; the reaction of peroxide radicals with 4-chloronaphthol produces a dark purple stain that can be photographed without using specialized photographic film.
1506:"Transfer of proteins from gels to diazobenzyloxymethyl-paper and detection with antisera: a method for studying antibody specificity and antigen structure"
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mesh of the gel. Smaller proteins migrate faster through this mesh, and the proteins are thus separated according to size (usually measured in kilodaltons,
150:
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2232:
695:
418:, electric charge, or a combination of these factors. The nature of the separation depends on the treatment of the sample and the nature of the gel.
194:
2339:"14-3-3 protein levels and isoform patterns in the cerebrospinal fluid of Creutzfeldt-Jakob disease patients in the progressive and terminal stages"
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is applied along the gel, proteins migrate through it at different speeds dependent on their size. These different rates of advancement (different
3781:
1230:
2773:"Production, Characterization, and Epitope Mapping of Monoclonal Antibodies Against Different Subtypes of Rabbit Hemorrhagic Disease Virus (RHDV)"
468:, which is a commercially available mixture of proteins of known molecular weights, typically stained so as to form visible, coloured bands. When
859:
western blot analysis. Fluorescence is considered to be one of the best methods for quantification but is less sensitive than chemiluminescence.
2092:"Application Note: Improved detection of EPO in blood and urine based on novel Velum SAR precast horizontal gels optimized for routine analysis"
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Reichel C, Benetka W, Lorenc B, Thevis M (November 2016). "Evaluation of AMGEN clone 9G8A anti-Epo antibody for application in doping control".
3306:
Harbers M (2015). "Shift-Western
Blotting: Separate Analysis of Protein and DNA from Protein–DNA Complexes". In Kurien BT, Scofield RH (eds.).
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Researchers use different software to process and align image-sections for elegant presentation of western blot results. Popular tools include
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Moritz CP, Marz SX, Reiss R, Schulenborg T, Friauf E (February 2014). "Epicocconone staining: a powerful loading control for
Western blots".
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The colorimetric detection method depends on incubation of the western blot with a substrate that reacts with the reporter enzyme (such as
3598:
Kiyatkin A, Aksamitiene E (2009). "Multistrip
Western Blotting to Increase Quantitative Data Output". In Kurien BT, Scofield RH (eds.).
4133:
4013:
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Wang, Yuji; Li, Dawei; Xu, Nanwei; Tao, Weijian; Zhu, Ruixia; Sun, Rongbin; Fan, Weiwei; Zhang, Ping; Dong, Tianhua; Yu, Long (2011).
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Wang, Yuji; Li, Dawei; Xu, Nanwei; Tao, Weijian; Zhu, Ruixia; Sun, Rongbin; Fan, Weiwei; Zhang, Ping; Dong, Tianhua; Yu, Long (2011).
3852:
3441:
Talmi-Frank D, Jaffe CL, Baneth G (2015). "Quantitative
Computerized Western Blotting in Detail". In Kurien BT, Scofield RH (eds.).
2282:"Lapatinib antagonizes multidrug resistance-associated protein 1-mediated multidrug resistance by inhibiting its transport function"
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2233:"Development of Idarubicin and Doxorubicin Solid Lipid Nanoparticles to Overcome Pgp-Mediated Multiple Drug Resistance in Leukemia"
1408:"Method for detection of specific RNAs in agarose gels by transfer to diazobenzyloxymethyl-paper and hybridization with DNA probes"
778:. This practice ensures correction for the amount of total protein on the membrane in case of errors or incomplete transfers. (see
770:
to the structural protein to control between groups. A superior strategy is the normalization to the total protein visualized with
2231:
Ma, Ping; Dong, Xiaowei; Swadley, Courtney L.; Gupte, Anshul; Leggas, Markos; Ledebur, Harry C.; Mumper, Russell J. (2009-04-01).
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Ingrosso L, Vetrugno V, Cardone F, Pocchiari M (June 2002). "Molecular diagnostics of transmissible spongiform encephalopathies".
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at which they have a neutral net charge) in the first dimension, and according to their molecular weight in the second dimension.
83:
is added which recognizes and binds to the primary antibody. The secondary antibody is visualized through various methods such as
2573:"Follistatin-like protein 1: a serum biochemical marker reflecting the severity of joint damage in patients with osteoarthritis"
2454:"Follistatin-like protein 1: a serum biochemical marker reflecting the severity of joint damage in patients with osteoarthritis"
4095:
2830:"Important considerations for protein analyses using antibody based techniques: down-sizing Western blotting up-sizes outcomes"
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that of the marker or ladder loaded during electrophoresis. The process is commonly repeated for a structural protein, such as
4252:
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3213:
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out on a microchip. 400 nanograms of cell lysate are all that is needed to identify and quantify eleven different proteins.
4197:
3196:
Kurien BT, Scofield RH (2015). "Other
Notable Protein Blotting Methods: A Brief Review". In Kurien BT, Scofield RH (eds.).
3249:"Western Blotting Inaccuracies with Unverified Antibodies: Need for a Western Blotting Minimal Reporting Standard (WBMRS)"
3814:
1568:"Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications"
886:
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takes place in a two-step process, although there are now one-step detection methods available for certain applications.
490:
3793:
658:
After rinsing the membrane to remove unbound primary antibody, the membrane is exposed to another antibody known as the
1796:"A novel screening ELISA and a confirmatory Western blot useful for diagnosis and epidemiological studies of tularemia"
115:
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3930:
659:
229:
210:
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Mathews ST, Plaisance EP, Kim T (2009). "Imaging Systems for Westerns: Chemiluminescence vs. Infrared Detection".
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Horseradish peroxidase is commonly linked to secondary antibodies to allow the detection of the target protein by
3911:
3700:
536:, bringing the proteins with it. In practice this method is not commonly used due to the lengthy procedure time.
486:. Protein bands can then be compared to the ladder bands, allowing estimation of the protein's molecular weight.
190:
3719:
4247:
4126:
2280:
Ma, Shao-lin; Hu, Ya-peng; Wang, Fang; Huang, Zhen-cong; Chen, Yi-fan; Wang, Xiao-kun; Fu, Li-wu (2014-09-08).
3940:
3845:
2673:
Barberis E, Marengo E, Manfredi M (2021). "Protein Subcellular Localization Prediction". In Cecconi D (ed.).
2630:
Lee YH, Tan HT, Chung MC (November 2010). "Subcellular fractionation methods and strategies for proteomics".
3970:
445:, and migrate towards the positively charged (higher voltage) anode (usually having a red wire) through the
4237:
3988:
925:
the detection system's software can address weak bands caused by lower sample and antibody concentrations.
493:
which spreads the proteins from a single sample out in two dimensions. Proteins are separated according to
335:
proteins by the length of the polypeptide, followed by an electrophoretic transfer onto a membrane (mostly
4087:
3993:
3921:
2514:"Differential proteomic analysis of synovial fluid from rheumatoid arthritis and osteoarthritis patients"
2395:"Differential proteomic analysis of synovial fluid from rheumatoid arthritis and osteoarthritis patients"
430:
332:
3396:
Eaton SL, Hurtado ML, Oldknow KJ, Graham LC, Marchant TW, Gillingwater TH, et al. (November 2014).
779:
767:
2338:
690:. The chemiluminescent substrate is cleaved by horseradish peroxidase, resulting in the production of
4119:
3945:
3935:
3925:
3887:
2979:
Welinder C, Ekblad L (March 2011). "Coomassie staining as loading control in Western blot analysis".
2879:"An overview of technical considerations for Western blotting applications to physiological research"
1146:
1006:
results, with the aid of more advanced imaging technologies and modern fluorescent labeling methods.
523:
4242:
3965:
3838:
3482:
Treindl F, Ruprecht B, Beiter Y, Schultz S, Döttinger A, Staebler A, et al. (September 2016).
3445:. Methods in Molecular Biology. Vol. 1312. New York, NY: Springer New York. pp. 141–150.
3310:. Methods in Molecular Biology. Vol. 1312. New York, NY: Springer New York. pp. 355–373.
3200:. Methods in Molecular Biology. Vol. 1312. New York, NY: Springer New York. pp. 487–503.
2931:"Tubulin or Not Tubulin: Heading Toward Total Protein Staining as Loading Control in Western Blots"
571:
473:
268:
255:
2930:
2337:
Shiga, Yusei; Wakabayashi, Hideki; Miyazawa, Koichi; Kido, Hiroshi; Itoyama, Yasuto (2006-07-01).
2176:"Auto-antibodies to vascular endothelial cadherin in humans: association with autoimmune diseases"
3810:
3789:
2008:"Antidoping programme and biological monitoring before and during the 2014 FIFA World Cup Brazil"
79:
is washed in a solution containing the primary antibody, before excess antibody is washed off. A
2877:
Bass JJ, Wilkinson DJ, Rankin D, Phillips BE, Szewczyk NJ, Smith K, Atherton PJ (January 2017).
4036:
3998:
680:
350:
3065:"Stain-Free total protein staining is a superior loading control to β-actin for Western blots"
2111:"Profiling protein expression in circulating tumour cells using microfluidic western blotting"
437:(e.g. disulfide bonds to sulfhydryl groups ) and thus allows separation of proteins by their
3955:
3775:
3398:"A guide to modern quantitative fluorescent western blotting with troubleshooting strategies"
2677:. Methods in Molecular Biology. Vol. 2361. New York, NY: Springer US. pp. 197–212.
1224:
232:(BSE, commonly referred to as 'mad cow disease'). Another application is in the diagnosis of
99:
76:
65:
4003:
3882:
3714:
3602:. Methods in Molecular Biology. Vol. 536. Totowa, NJ: Humana Press. pp. 149–161.
3552:
3495:
3260:
3015:
2784:
2122:
1579:
1517:
1419:
986:
676:
600:
592:
103:
40:
1932:
Golden MR, Ashley-Morrow R, Swenson P, Hogrefe WR, Handsfield HH, Wald A (December 2005).
749:
228:, a type of prion disease linked to the consumption of contaminated beef from cattle with
8:
3916:
3907:
3819:
407:
393:
328:
242:
revealed that its sensitivity is almost 100% and the specificity is 99.6%. Some forms of
107:
3556:
3499:
3264:
2788:
2126:
1583:
1521:
1423:
349:(SDS-PAGE) is generally used for the denaturing electrophoretic separation of proteins.
343:) and an immunostaining procedure to visualize a certain protein on the blot membrane.
216:
The confirmatory HIV test employs a western blot to detect anti-HIV antibody in a human
3902:
3758:
3731:
3675:
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3540:
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2572:
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2513:
2488:
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2314:
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2213:
2151:
2110:
2032:
2007:
1963:
1950:
1933:
1871:
1844:
1820:
1795:
1695:
1670:
1383:
1358:
1326:
1207:
1180:
667:
To allow detection of the target protein, the secondary antibody is commonly linked to
441:. Sampled proteins become covered in the negatively charged SDS, effectively becoming
434:
198:
88:
80:
61:
1772:
1602:
1567:
1540:
1505:
1442:
1407:
4215:
4191:
4057:
3763:
3680:
3631:
3611:
3580:
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3454:
3423:
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3329:
3319:
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3229:
3209:
3178:
3168:
3141:
3129:
3094:
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2953:
2908:
2859:
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2745:
2708:
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2612:
2594:
2553:
2535:
2493:
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2434:
2416:
2366:
2358:
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2301:
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2197:
2156:
2138:
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1955:
1907:
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1700:
1651:
1607:
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1318:
1212:
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990:
908:
893:
799:
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687:
494:
411:
44:
2965:
2659:
2378:
2217:
2006:
Baume N, Jan N, Emery C, Mandanis B, Schweizer C, Giraud S, et al. (May 2015).
1967:
189:
for the qualitative detection of single proteins and protein-modifications (such as
173:
4209:
4203:
4072:
3753:
3743:
3670:
3662:
3649:
Jin S, Furtaw MD, Chen H, Lamb DT, Ferguson SA, Arvin NE, et al. (July 2016).
3621:
3603:
3570:
3560:
3511:
3503:
3446:
3413:
3405:
3368:
3360:
3311:
3278:
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2543:
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2064:
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2019:
1945:
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1427:
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1308:
1202:
1192:
1141:
1136:
1123:
962:
897:
771:
637:
533:
415:
372:
165:-listed publications" and may still be the most used protein-analytical technique.
72:
2757:
1794:
Schmitt P, Splettstösser W, Porsch-Ozcürümez M, Finke EJ, Grunow R (August 2005).
1374:
181:
where first two strips are negative and positive controls followed by actual tests
4142:
4041:
3865:
3830:
3666:
3607:
3450:
3315:
3273:
3205:
3164:
2845:
2682:
2023:
855:
575:
529:
354:
91:, and radioactivity, allowing indirect detection of the specific target protein.
3484:"A bead-based western for high-throughput cellular signal transduction analyses"
1646:
1629:
1359:"Protein purification and analysis: next generation Western blotting techniques"
3980:
3897:
3545:
Proceedings of the National Academy of Sciences of the United States of America
3159:. Methods in Molecular Biology. Vol. 536. Humana Press. pp. 499–513.
2354:
2192:
2175:
1572:
Proceedings of the National Academy of Sciences of the United States of America
1510:
Proceedings of the National Academy of Sciences of the United States of America
1412:
Proceedings of the National Academy of Sciences of the United States of America
1095:
896:, while in the second dimension, polypeptides are separated according to their
723:
558:
519:
438:
426:
422:
340:
289:
264:
134:
111:
48:
3798:
2297:
1811:
832:
4231:
4162:
4156:
4077:
4067:
4008:
3748:
3080:
2740:
2723:
2598:
2539:
2479:
2420:
2362:
2305:
2201:
2142:
1197:
596:
238:
138:
126:
3565:
2724:"Epitope mapping of antibodies using a cell array-based polypeptide library"
2107:
1736:
1719:
1432:
319:
4174:
4062:
4031:
3767:
3684:
3635:
3584:
3525:
3468:
3427:
3382:
3333:
3292:
3233:
3182:
3133:
3125:
3098:
3000:
2957:
2949:
2912:
2863:
2814:
2749:
2700:
2651:
2643:
2616:
2557:
2530:
2497:
2438:
2411:
2370:
2323:
2266:
2209:
2160:
2076:
2041:
1959:
1895:
1880:
1829:
1780:
1745:
1704:
1655:
1592:
1530:
1392:
1322:
1297:"Western blotting: a powerful staple in scientific and biomedical research"
1216:
1131:
795:
775:
738:
691:
608:
567:
398:
259:
243:
236:. An evaluation of the western blot's ability to detect antibodies against
217:
186:
142:
3049:
2248:
1981:
1911:
1861:
1487:
1313:
1296:
766:, that should not change between samples. The amount of target protein is
254:
Further applications of the western blot technique include its use by the
1793:
1686:
1611:
1451:
1072:
837:
277:
158:
75:) is created that recognizes and binds to a specific target protein. The
3507:
3247:
Gilda JE, Ghosh R, Cheah JX, West TM, Bodine SC, Gomes AV (2015-08-19).
2771:
Kong D, Liu J, Jiang Q, Yu Z, Hu X, Guo D, et al. (February 2016).
2134:
1671:"Human Immunodeficiency Virus Diagnostic Testing: 30 Years of Evolution"
1549:
509:
19:
3874:
3364:
3347:
Hughes AJ, Spelke DP, Xu Z, Kang CC, Schaffer DV, Herr AE (July 2014).
846:
811:
791:
603:(TBS) or I-Block, with a minute percentage (0.1%) of detergent such as
548:
446:
110:, where antibodies are used to detect proteins in tissues and cells by
2992:
2894:
2796:
2722:
Maier RH, Maier CJ, Rid R, Hintner H, Bauer JW, Onder K (April 2010).
2510:
2391:
591:
placing the membrane in a dilute solution of protein – typically 3–5%
296:
2068:
871:
663:
563:
362:
233:
149:, and by Harry Towbin, Theophil Staehelin, and Julian Gordon at the
4111:
2589:
2470:
1089:
904:
841:
619:
604:
367:
358:
206:
178:
146:
95:
84:
68:
52:
3409:
1103:
3861:
1931:
955:
763:
706:
579:
469:
442:
202:
1758:
1027:
672:
668:
162:
3651:"Multiplexed Western Blotting Using Microchip Electrophoresis"
1894:
De Castro L, Yoshida CF, Gaspar AM, Gomes SA (December 1996).
4023:
759:
710:
154:
3481:
2336:
2876:
1893:
994:
421:
By far the most common type of gel electrophoresis employs
336:
3111:
2173:
2054:
1045:
3395:
1036:
662:. Antibodies come from animal sources (or animal sourced
450:
347:
Sodium dodecyl sulfate–polyacrylamide gel electrophoresis
248:
221:
130:
3820:"Blotting Techniques/ The Principle of Western Blotting"
2883:
Scandinavian Journal of Medicine & Science in Sports
1724:
Indian Journal of Dermatology, Venereology and Leprology
1630:"40 years Western blotting: A scientific birthday toast"
3732:"Western blot: technique, theory, and trouble shooting"
2672:
1181:"Western blot: technique, theory, and trouble shooting"
498:
205:. It is also used in medical diagnostics, e.g., in the
3440:
1845:"Western Blot as a confirmatory test for Lyme disease"
1294:
1073:
Microchip capillary electrophoresis-based western blot
133:
detection named after its inventor, English biologist
3016:"Improving quantification accuracy for western blots"
2005:
1565:
3826:. Biomedical and Biological Sciences. 23 March 2017.
2721:
1085:
982:
3597:
3246:
3154:
297:
Identification of protein localization across cells
3860:
3346:
2230:
1566:Towbin H, Staehelin T, Gordon J (September 1979).
872:Minimum requirement specification for Western Blot
557:with the so-called "loading control" was based on
3648:
1503:
1356:
728:combined with optical software (e.g. Optiquant).
4229:
1717:
914:
331:to separate native proteins by 3-D structure or
1405:
1295:Begum H, Murugesan P, Tangutur AD (June 2022).
460:in the gel. One lane is usually reserved for a
406:The proteins of the sample are separated using
3195:
2978:
2924:
2922:
2770:
1406:Alwine JC, Kemp DJ, Stark GR (December 1977).
1357:Mishra M, Tiwari S, Gomes AV (November 2017).
970:
956:Improvements for Western Blot Related Problems
744:
16:Analytical technique used in molecular biology
4127:
3846:
3035:
2279:
1669:Alexander TS (April 2016). Pasetti MF (ed.).
966:
946:
805:
3780:: CS1 maint: DOI inactive as of July 2024 (
1999:
1623:
1621:
1561:
1559:
1499:
1497:
1229:: CS1 maint: DOI inactive as of July 2024 (
1054:
1028:Quantifiable fluorescence-based western blot
3729:
2919:
2629:
2570:
2451:
2048:
1849:The Canadian Journal of Infectious Diseases
1458:
1178:
1018:
911:, which identifies their molecular weight.
137:. Similarly, detection of RNA is termed as
4134:
4120:
3853:
3839:
3736:North American Journal of Medical Sciences
3538:
3062:
3007:
2827:
1504:Renart J, Reiser J, Stark GR (July 1979).
1185:North American Journal of Medical Sciences
1063:
880:
3757:
3747:
3674:
3625:
3574:
3564:
3515:
3417:
3372:
3282:
3272:
3223:
3088:
3013:
2902:
2853:
2804:
2739:
2606:
2588:
2547:
2529:
2487:
2469:
2428:
2410:
2313:
2256:
2191:
2150:
2031:
1949:
1870:
1860:
1819:
1735:
1694:
1668:
1645:
1618:
1601:
1591:
1556:
1539:
1529:
1494:
1441:
1431:
1382:
1312:
1206:
1196:
928:
785:
543:
3805:. Bio-Rad Laboratories. 16 October 2012.
3036:Stennert E, Arold R (October 1973). "".
2089:
1464:
1399:
1000:
831:
827:
818:
748:
618:
547:
508:
397:
318:
185:The western blot is extensively used in
172:
18:
4212:(lipid:post translational modification)
3305:
1720:"Western blot profile in HIV infection"
1046:High-throughput western blot (DigiWest)
971:automated microfluidic western blotting
967:single-cell resolution western blotting
753:Western blot chemiluminescent detection
327:The western blot method is composed of
4230:
4096:Photoactivated localization microscopy
4014:Protein–protein interaction prediction
2928:
1842:
1627:
1037:Quantitative computerized western blot
387:
4115:
3834:
3730:Mahmood T, Yang PC (September 2012).
3063:Gilda JE, Gomes AV (September 2013).
1290:
1288:
1286:
1284:
1282:
1280:
1278:
1276:
1274:
1272:
1270:
1268:
1266:
1264:
1262:
1260:
1179:Mahmood T, Yang PC (September 2012).
1009:
919:
653:
566:, stain-free techniques, Sypro Ruby,
378:
4198:Electrophoretic mobility shift assay
4141:
3539:Hughes AJ, Herr AE (December 2012).
2828:Murphy RM, Lamb GD (December 2013).
2237:Journal of Biomedical Nanotechnology
1718:Sudha T, Lakshmi V, Teja VD (2006).
1352:
1350:
1348:
1346:
1344:
1342:
1340:
1258:
1256:
1254:
1252:
1250:
1248:
1246:
1244:
1242:
1240:
1174:
1172:
1170:
1168:
1166:
862:
844:-dye labelled secondary antibody in
410:. Separation of proteins may be by
3971:Freeze-fracture electron microscopy
887:Two-dimensional gel electrophoresis
631:
13:
2012:British Journal of Sports Medicine
1951:10.1097/01.olq.0000175377.88358.f3
937:
305:
14:
4264:
4177:(post translational modification)
3694:
3402:Journal of Visualized Experiments
2728:Journal of Biomolecular Screening
1337:
1237:
1163:
226:variant Creutzfeldt–Jakob disease
116:enzyme-linked immunosorbent assay
94:Other related techniques include
3951:Isothermal titration calorimetry
3931:Dual-polarization interferometry
2577:Arthritis Research & Therapy
2458:Arthritis Research & Therapy
2343:Journal of Clinical Neuroscience
1116:
1102:
1088:
230:bovine spongiform encephalopathy
191:post-translational modifications
3642:
3591:
3541:"Microfluidic Western blotting"
3532:
3475:
3434:
3389:
3340:
3299:
3240:
3189:
3148:
3105:
3056:
3029:
2972:
2870:
2821:
2764:
2715:
2666:
2623:
2564:
2504:
2445:
2385:
2330:
2273:
2224:
2167:
2101:
2083:
1974:
1925:
1887:
1836:
1787:
1752:
1711:
1675:Clinical and Vaccine Immunology
976:
168:
3600:Protein Blotting and Detection
3349:"Single-cell western blotting"
3157:Protein Blotting and Detection
1662:
798:(how intense the stain is) or
1:
3941:Chromatin immunoprecipitation
1938:Sexually Transmitted Diseases
1773:10.1016/S1471-4914(02)02358-4
1375:10.1080/14789450.2017.1388167
1157:
915:Western Blot Related Problems
614:
489:It is also possible to use a
353:(SDS) is generally used as a
4253:Molecular biology techniques
4004:Protein structural alignment
3989:Protein structure prediction
3720:Resources in other libraries
3667:10.1021/acs.analchem.6b00705
3608:10.1007/978-1-59745-542-8_17
3451:10.1007/978-1-4939-2694-7_18
3316:10.1007/978-1-4939-2694-7_36
3274:10.1371/journal.pone.0135392
3206:10.1007/978-1-4939-2694-7_51
3165:10.1007/978-1-59745-542-8_51
2981:Journal of Proteome Research
2846:10.1113/jphysiol.2013.263251
2683:10.1007/978-1-0716-1641-3_12
2024:10.1136/bjsports-2015-094762
1982:"FIV testing – which to use"
1761:Trends in Molecular Medicine
1480:10.1016/0003-2697(81)90281-5
314:
220:sample. Proteins from known
151:Friedrich Miescher Institute
7:
4088:Super-resolution microscopy
3994:Protein function prediction
3922:Peptide mass fingerprinting
3917:Protein immunoprecipitation
1647:10.1016/j.jprot.2019.103575
1628:Moritz CP (February 2020).
1363:Expert Review of Proteomics
1081:
836:Western blot using an anti-
745:Detection and visualization
731:
585:
504:
10:
4269:
2929:Moritz CP (October 2017).
2355:10.1016/j.jocn.2005.09.004
2193:10.1038/labinvest.2013.106
1800:Epidemiology and Infection
947:Irregular and uneven bands
884:
806:Chemiluminescent detection
780:western blot normalization
599:(both are inexpensive) in
475:electrophoretic mobilities
391:
4184:
4149:
4086:
4050:
4022:
3979:
3946:Surface plasmon resonance
3936:Microscale thermophoresis
3926:Protein mass spectrometry
3888:Green fluorescent protein
3873:
3715:Resources in your library
2834:The Journal of Physiology
2298:10.2119/molmed.2014.00059
2057:Drug Testing and Analysis
1812:10.1017/s0950268805003742
1147:Fast parallel proteolysis
1055:Microfluidic western blot
524:polyvinylidene difluoride
269:synthetic oxygen carriers
3966:Cryo-electron microscopy
3749:10.4103/1947-2714.100998
3081:10.1016/j.ab.2013.05.027
3014:Ambroz K. (2006-09-20).
2741:10.1177/1087057110363821
2675:Proteomics Data Analysis
2180:Laboratory Investigation
1198:10.4103/1947-2714.100998
1019:Single-cell western blot
840:primary antibody and an
456:Samples are loaded into
402:SDS-PAGE electrophoresis
256:World Anti-Doping Agency
77:electrophoresis membrane
3999:Protein–protein docking
3912:Protein electrophoresis
3752:(inactive 2024-07-09).
3566:10.1073/pnas.1207754110
3069:Analytical Biochemistry
1843:Artsob H (March 1993).
1737:10.4103/0378-6323.27752
1468:Analytical Biochemistry
1433:10.1073/pnas.74.12.5350
1201:(inactive 2024-07-09).
1064:Multistrip western blot
881:2-D gel electrophoresis
323:From gel to publication
3898:Protein immunostaining
3706:Western immunoblotting
3126:10.1002/pmic.201300089
2950:10.1002/pmic.201600189
2644:10.1002/pmic.201000289
2531:10.1186/1559-0275-11-1
2412:10.1186/1559-0275-11-1
1593:10.1073/pnas.76.9.4350
1531:10.1073/pnas.76.7.3116
965:, diffusion blotting,
929:Multiple band problems
851:
786:Colorimetric detection
754:
681:horseradish peroxidase
624:
553:
544:Total protein staining
514:
403:
351:Sodium dodecyl sulfate
324:
274:Laboratory of Lausanne
182:
31:(sometimes called the
24:
4248:Laboratory techniques
3956:X-ray crystallography
3488:Nature Communications
2249:10.1166/jbn.2009.1021
2115:Nature Communications
1634:Journal of Proteomics
1314:10.2144/btn-2022-0003
1001:Enhanced Western Blot
856:fluorescently labeled
835:
828:Fluorescent detection
819:Radioactive detection
752:
622:
551:
513:Western blot transfer
512:
401:
322:
176:
100:quantitative dot blot
23:Western blot workflow
22:
3883:Protein purification
3655:Analytical Chemistry
2063:(11–12): 1131–1137.
1687:10.1128/CVI.00053-16
987:Microsoft PowerPoint
963:far-western blotting
677:alkaline phosphatase
601:tris-buffered saline
593:bovine serum albumin
552:Western blot binding
104:immunohistochemistry
41:analytical technique
4238:Diagnostic virology
3908:Gel electrophoresis
3557:2012PNAS..10921450H
3551:(52): 21450–21455.
3508:10.1038/ncomms12852
3500:2016NatCo...712852T
3265:2015PLoSO..1035392G
2789:2016NatSR...620857K
2518:Clinical Proteomics
2399:Clinical Proteomics
2135:10.1038/ncomms14622
2127:2017NatCo...814622S
2090:Schwenke D (2015).
1862:10.1155/1993/796390
1584:1979PNAS...76.4350T
1522:1979PNAS...76.3116R
1424:1977PNAS...74.5350A
491:two-dimensional gel
408:gel electrophoresis
394:Gel electrophoresis
388:Gel electrophoresis
329:gel electrophoresis
147:Stanford University
108:immunocytochemistry
51:to detect specific
39:, is a widely used
4051:Display techniques
3903:Protein sequencing
3799:"Western Blotting"
3365:10.1038/nmeth.2992
2777:Scientific Reports
2286:Molecular Medicine
1010:Shift-western blot
920:Detection problems
852:
755:
660:secondary antibody
654:Secondary antibody
638:primary antibodies
625:
554:
515:
435:tertiary structure
404:
379:Sample Preparation
325:
251:+ status in cats.
199:protein production
183:
129:, a technique for
89:immunofluorescence
81:secondary antibody
33:protein immunoblot
25:
4225:
4224:
4216:Northwestern blot
4206:(protein:protein)
4192:Southwestern blot
4109:
4108:
4058:Bacterial display
3701:Library resources
3661:(13): 6703–6710.
3617:978-1-934115-73-2
3460:978-1-4939-2693-0
3325:978-1-4939-2693-0
3215:978-1-4939-2693-0
3174:978-1-934115-73-2
2993:10.1021/pr1011476
2895:10.1111/sms.12702
2840:(23): 5823–5831.
2797:10.1038/srep20857
2692:978-1-0716-1640-6
2638:(22): 3935–3956.
2186:(11): 1194–1202.
1418:(12): 5350–5354.
1369:(11): 1037–1053.
1152:Northwestern blot
1110:Technology portal
991:Adobe Illustrator
909:mass spectrometry
894:isoelectric point
863:Secondary probing
800:spectrophotometry
700:hydrogen peroxide
688:chemiluminescence
495:isoelectric point
412:isoelectric point
125:is a play on the
45:molecular biology
4260:
4210:Far-eastern blot
4204:Far-western blot
4143:Molecular probes
4136:
4129:
4122:
4113:
4112:
4073:Ribosome display
4009:Protein ontology
3855:
3848:
3841:
3832:
3831:
3827:
3806:
3785:
3779:
3771:
3761:
3751:
3689:
3688:
3678:
3646:
3640:
3639:
3629:
3595:
3589:
3588:
3578:
3568:
3536:
3530:
3529:
3519:
3479:
3473:
3472:
3443:Western Blotting
3438:
3432:
3431:
3421:
3393:
3387:
3386:
3376:
3344:
3338:
3337:
3308:Western Blotting
3303:
3297:
3296:
3286:
3276:
3244:
3238:
3237:
3227:
3198:Western Blotting
3193:
3187:
3186:
3152:
3146:
3145:
3120:(2–3): 162–168.
3109:
3103:
3102:
3092:
3060:
3054:
3053:
3033:
3027:
3026:
3020:
3011:
3005:
3004:
2987:(3): 1416–1419.
2976:
2970:
2969:
2935:
2926:
2917:
2916:
2906:
2874:
2868:
2867:
2857:
2825:
2819:
2818:
2808:
2768:
2762:
2761:
2743:
2719:
2713:
2712:
2670:
2664:
2663:
2627:
2621:
2620:
2610:
2592:
2568:
2562:
2561:
2551:
2533:
2508:
2502:
2501:
2491:
2473:
2449:
2443:
2442:
2432:
2414:
2389:
2383:
2382:
2334:
2328:
2327:
2317:
2277:
2271:
2270:
2260:
2228:
2222:
2221:
2195:
2171:
2165:
2164:
2154:
2105:
2099:
2098:
2096:
2087:
2081:
2080:
2069:10.1002/dta.2057
2052:
2046:
2045:
2035:
2003:
1997:
1996:
1994:
1992:
1978:
1972:
1971:
1953:
1929:
1923:
1922:
1920:
1918:
1906:(5–6): 251–258.
1891:
1885:
1884:
1874:
1864:
1840:
1834:
1833:
1823:
1791:
1785:
1784:
1756:
1750:
1749:
1739:
1715:
1709:
1708:
1698:
1666:
1660:
1659:
1649:
1625:
1616:
1615:
1605:
1595:
1578:(9): 4350–4354.
1563:
1554:
1553:
1543:
1533:
1516:(7): 3116–3120.
1501:
1492:
1491:
1462:
1456:
1455:
1445:
1435:
1403:
1397:
1396:
1386:
1354:
1335:
1334:
1316:
1292:
1235:
1234:
1228:
1220:
1210:
1200:
1176:
1142:Far-western blot
1137:Far-eastern blot
1126:
1124:Chemistry portal
1121:
1120:
1119:
1112:
1107:
1106:
1098:
1093:
1092:
898:molecular weight
772:trichloroethanol
696:4-chloronaphthol
632:Primary antibody
597:non-fat dry milk
534:capillary action
478:) separate into
416:molecular weight
373:cross-reactivity
73:primary antibody
37:western blotting
4268:
4267:
4263:
4262:
4261:
4259:
4258:
4257:
4243:Protein methods
4228:
4227:
4226:
4221:
4180:
4145:
4140:
4110:
4105:
4082:
4046:
4042:Secretion assay
4018:
3975:
3869:
3859:
3818:
3815:Wayback Machine
3797:
3794:Wayback Machine
3773:
3772:
3726:
3725:
3724:
3709:
3708:
3704:
3697:
3692:
3647:
3643:
3618:
3596:
3592:
3537:
3533:
3480:
3476:
3461:
3439:
3435:
3394:
3390:
3345:
3341:
3326:
3304:
3300:
3259:(8): e0135392.
3245:
3241:
3216:
3194:
3190:
3175:
3153:
3149:
3110:
3106:
3061:
3057:
3044:(10): 293–296.
3034:
3030:
3018:
3012:
3008:
2977:
2973:
2944:(20): 1600189.
2933:
2927:
2920:
2875:
2871:
2826:
2822:
2769:
2765:
2720:
2716:
2693:
2671:
2667:
2628:
2624:
2569:
2565:
2509:
2505:
2450:
2446:
2390:
2386:
2335:
2331:
2278:
2274:
2229:
2225:
2172:
2168:
2106:
2102:
2094:
2088:
2084:
2053:
2049:
2004:
2000:
1990:
1988:
1980:
1979:
1975:
1944:(12): 771–777.
1930:
1926:
1916:
1914:
1900:Acta Virologica
1892:
1888:
1841:
1837:
1792:
1788:
1757:
1753:
1716:
1712:
1667:
1663:
1626:
1619:
1564:
1557:
1502:
1495:
1463:
1459:
1404:
1400:
1355:
1338:
1293:
1238:
1222:
1221:
1177:
1164:
1160:
1122:
1117:
1115:
1108:
1101:
1094:
1087:
1084:
1075:
1066:
1057:
1048:
1039:
1030:
1021:
1012:
1003:
979:
958:
949:
940:
938:High background
931:
922:
917:
889:
883:
874:
865:
850:major extracts.
830:
821:
808:
788:
747:
734:
656:
634:
623:Probing process
617:
588:
572:Coomassie R-350
546:
530:electroblotting
507:
427:reducing agents
396:
390:
381:
375:of antibodies.
317:
308:
306:Epitope mapping
299:
195:dilution series
171:
17:
12:
11:
5:
4266:
4256:
4255:
4250:
4245:
4240:
4223:
4222:
4220:
4219:
4213:
4207:
4201:
4195:
4188:
4186:
4182:
4181:
4179:
4178:
4172:
4166:
4160:
4153:
4151:
4147:
4146:
4139:
4138:
4131:
4124:
4116:
4107:
4106:
4104:
4103:
4098:
4092:
4090:
4084:
4083:
4081:
4080:
4075:
4070:
4065:
4060:
4054:
4052:
4048:
4047:
4045:
4044:
4039:
4034:
4028:
4026:
4020:
4019:
4017:
4016:
4011:
4006:
4001:
3996:
3991:
3985:
3983:
3981:Bioinformatics
3977:
3976:
3974:
3973:
3968:
3963:
3958:
3953:
3948:
3943:
3938:
3933:
3928:
3919:
3914:
3905:
3900:
3895:
3890:
3885:
3879:
3877:
3871:
3870:
3858:
3857:
3850:
3843:
3835:
3829:
3828:
3807:
3786:
3742:(9): 429–434.
3723:
3722:
3717:
3711:
3710:
3699:
3698:
3696:
3695:External links
3693:
3691:
3690:
3641:
3616:
3590:
3531:
3474:
3459:
3433:
3404:(93): e52099.
3388:
3359:(7): 749–755.
3353:Nature Methods
3339:
3324:
3298:
3239:
3214:
3188:
3173:
3147:
3104:
3075:(2): 186–188.
3055:
3028:
3023:Image Analysis
3006:
2971:
2918:
2869:
2820:
2763:
2734:(4): 418–426.
2714:
2691:
2665:
2622:
2590:10.1186/ar3522
2563:
2503:
2471:10.1186/ar3522
2444:
2384:
2349:(6): 661–665.
2329:
2292:(1): 390–399.
2272:
2243:(2): 151–161.
2223:
2166:
2100:
2082:
2047:
2018:(9): 614–622.
1998:
1973:
1924:
1886:
1855:(2): 115–116.
1835:
1806:(4): 759–766.
1786:
1767:(6): 273–280.
1751:
1730:(5): 357–360.
1710:
1681:(4): 249–253.
1661:
1617:
1555:
1493:
1474:(2): 195–203.
1457:
1398:
1336:
1236:
1191:(9): 429–434.
1161:
1159:
1156:
1155:
1154:
1149:
1144:
1139:
1134:
1128:
1127:
1113:
1099:
1096:Biology portal
1083:
1080:
1074:
1071:
1065:
1062:
1056:
1053:
1047:
1044:
1038:
1035:
1029:
1026:
1020:
1017:
1011:
1008:
1002:
999:
978:
975:
957:
954:
948:
945:
939:
936:
930:
927:
921:
918:
916:
913:
885:Main article:
882:
879:
873:
870:
864:
861:
829:
826:
820:
817:
807:
804:
787:
784:
746:
743:
733:
730:
724:Staphylococcus
698:stain with 1%
671:or a reporter
655:
652:
633:
630:
616:
613:
587:
584:
559:immunostaining
545:
542:
520:nitrocellulose
506:
503:
439:molecular mass
423:polyacrylamide
392:Main article:
389:
386:
380:
377:
341:nitrocellulose
316:
313:
307:
304:
298:
295:
290:synovial fluid
265:erythropoietin
170:
167:
135:Edwin Southern
112:immunostaining
71:(known as the
66:animal-derived
49:immunogenetics
15:
9:
6:
4:
3:
2:
4265:
4254:
4251:
4249:
4246:
4244:
4241:
4239:
4236:
4235:
4233:
4218:(RNA:protein)
4217:
4214:
4211:
4208:
4205:
4202:
4200:(DNA:protein)
4199:
4196:
4194:(protein:DNA)
4193:
4190:
4189:
4187:
4183:
4176:
4173:
4170:
4167:
4164:
4163:Northern blot
4161:
4158:
4157:Southern blot
4155:
4154:
4152:
4148:
4144:
4137:
4132:
4130:
4125:
4123:
4118:
4117:
4114:
4102:
4099:
4097:
4094:
4093:
4091:
4089:
4085:
4079:
4078:Yeast display
4076:
4074:
4071:
4069:
4068:Phage display
4066:
4064:
4061:
4059:
4056:
4055:
4053:
4049:
4043:
4040:
4038:
4037:Protein assay
4035:
4033:
4030:
4029:
4027:
4025:
4021:
4015:
4012:
4010:
4007:
4005:
4002:
4000:
3997:
3995:
3992:
3990:
3987:
3986:
3984:
3982:
3978:
3972:
3969:
3967:
3964:
3962:
3959:
3957:
3954:
3952:
3949:
3947:
3944:
3942:
3939:
3937:
3934:
3932:
3929:
3927:
3923:
3920:
3918:
3915:
3913:
3909:
3906:
3904:
3901:
3899:
3896:
3894:
3891:
3889:
3886:
3884:
3881:
3880:
3878:
3876:
3872:
3867:
3863:
3856:
3851:
3849:
3844:
3842:
3837:
3836:
3833:
3825:
3821:
3816:
3812:
3808:
3804:
3800:
3795:
3791:
3787:
3783:
3777:
3769:
3765:
3760:
3755:
3750:
3745:
3741:
3737:
3733:
3728:
3727:
3721:
3718:
3716:
3713:
3712:
3707:
3702:
3686:
3682:
3677:
3672:
3668:
3664:
3660:
3656:
3652:
3645:
3637:
3633:
3628:
3623:
3619:
3613:
3609:
3605:
3601:
3594:
3586:
3582:
3577:
3572:
3567:
3562:
3558:
3554:
3550:
3546:
3542:
3535:
3527:
3523:
3518:
3513:
3509:
3505:
3501:
3497:
3493:
3489:
3485:
3478:
3470:
3466:
3462:
3456:
3452:
3448:
3444:
3437:
3429:
3425:
3420:
3415:
3411:
3410:10.3791/52099
3407:
3403:
3399:
3392:
3384:
3380:
3375:
3370:
3366:
3362:
3358:
3354:
3350:
3343:
3335:
3331:
3327:
3321:
3317:
3313:
3309:
3302:
3294:
3290:
3285:
3280:
3275:
3270:
3266:
3262:
3258:
3254:
3250:
3243:
3235:
3231:
3226:
3221:
3217:
3211:
3207:
3203:
3199:
3192:
3184:
3180:
3176:
3170:
3166:
3162:
3158:
3151:
3143:
3139:
3135:
3131:
3127:
3123:
3119:
3115:
3108:
3100:
3096:
3091:
3086:
3082:
3078:
3074:
3070:
3066:
3059:
3051:
3047:
3043:
3039:
3032:
3024:
3017:
3010:
3002:
2998:
2994:
2990:
2986:
2982:
2975:
2967:
2963:
2959:
2955:
2951:
2947:
2943:
2939:
2932:
2925:
2923:
2914:
2910:
2905:
2900:
2896:
2892:
2888:
2884:
2880:
2873:
2865:
2861:
2856:
2851:
2847:
2843:
2839:
2835:
2831:
2824:
2816:
2812:
2807:
2802:
2798:
2794:
2790:
2786:
2782:
2778:
2774:
2767:
2759:
2755:
2751:
2747:
2742:
2737:
2733:
2729:
2725:
2718:
2710:
2706:
2702:
2698:
2694:
2688:
2684:
2680:
2676:
2669:
2661:
2657:
2653:
2649:
2645:
2641:
2637:
2633:
2626:
2618:
2614:
2609:
2604:
2600:
2596:
2591:
2586:
2582:
2578:
2574:
2567:
2559:
2555:
2550:
2545:
2541:
2537:
2532:
2527:
2523:
2519:
2515:
2507:
2499:
2495:
2490:
2485:
2481:
2477:
2472:
2467:
2463:
2459:
2455:
2448:
2440:
2436:
2431:
2426:
2422:
2418:
2413:
2408:
2404:
2400:
2396:
2388:
2380:
2376:
2372:
2368:
2364:
2360:
2356:
2352:
2348:
2344:
2340:
2333:
2325:
2321:
2316:
2311:
2307:
2303:
2299:
2295:
2291:
2287:
2283:
2276:
2268:
2264:
2259:
2254:
2250:
2246:
2242:
2238:
2234:
2227:
2219:
2215:
2211:
2207:
2203:
2199:
2194:
2189:
2185:
2181:
2177:
2170:
2162:
2158:
2153:
2148:
2144:
2140:
2136:
2132:
2128:
2124:
2120:
2116:
2112:
2104:
2093:
2086:
2078:
2074:
2070:
2066:
2062:
2058:
2051:
2043:
2039:
2034:
2029:
2025:
2021:
2017:
2013:
2009:
2002:
1987:
1983:
1977:
1969:
1965:
1961:
1957:
1952:
1947:
1943:
1939:
1935:
1928:
1913:
1909:
1905:
1901:
1897:
1890:
1882:
1878:
1873:
1868:
1863:
1858:
1854:
1850:
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260:Blood doping
253:
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184:
169:Applications
143:George Stark
123:western blot
122:
120:
93:
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28:
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3961:Protein NMR
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838:lipoic acid
812:CCD cameras
576:Amido Black
278:Switzerland
272:accredited
159:Switzerland
4232:Categories
3114:Proteomics
2938:Proteomics
2632:Proteomics
1991:6 December
1917:6 December
1640:: 103575.
1158:References
847:Leishmania
792:peroxidase
768:normalized
615:Incubation
447:acrylamide
429:to remove
368:antibodies
98:analysis,
4171:(protein)
3142:206368546
2709:235768807
2599:1478-6354
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2421:1542-6416
2363:0967-5868
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2143:2041-1723
1331:250175915
664:hybridoma
595:(BSA) or
564:Ponceau S
431:secondary
363:Ponceau S
359:proteases
333:denatured
315:Procedure
234:tularemia
121:The name
118:(ELISA).
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3868:of study
3862:Proteins
3813:and the
3792:and the
3768:23050259
3685:27270033
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1960:16314775
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1830:16050523
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1393:28974114
1323:35775367
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1082:See also
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732:One step
675:such as
605:Tween 20
586:Blocking
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505:Transfer
258:(WADA).
207:HIV test
179:HIV test
96:dot blot
85:staining
69:antibody
53:proteins
4150:General
3866:methods
3824:YouTube
3803:YouTube
3759:3456489
3676:5113996
3627:2923389
3576:3535594
3553:Bibcode
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3496:Bibcode
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1420:Bibcode
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1964:S2CID
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1327:S2CID
760:actin
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1195::
1189:4
647:°
645:4
497:(
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