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 Table of Contents  
TECHNICAL ARTICLE
Year : 2012  |  Volume : 4  |  Issue : 9  |  Page : 429-434

Western blot: Technique, theory, and trouble shooting

Tahrin Mahmood, Ping-Chang Yang
Department of Pathology and Molecular Medicine, McMaster University, Hamilton, ON, Canada

Date of Web Publication14-Sep-2012

Correspondence Address:
Ping-Chang Yang
Department of Pathology & Molecular Medicine, McMaster University, Room T3303, 50 Charlton Ave East, Hamilton, ON
Canada
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Source of Support: None, Conflict of Interest: None


DOI: 10.4103/1947-2714.100998

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  Abstract 

Western blotting is an important technique used in cell and molecular biology. By using a western blot, researchers are able to identify specific proteins from a complex mixture of proteins extracted from cells. The technique uses three elements to accomplish this task: (1) separation by size, (2) transfer to a solid support, and (3) marking target protein using a proper primary and secondary antibody to visualize. This paper will attempt to explain the technique and theory behind western blot, and offer some ways to troubleshoot.

Keywords: Bio-medical research, protein, western blot


How to cite this article:
Mahmood T, Yang PC. Western blot: Technique, theory, and trouble shooting. North Am J Med Sci 2012;4:429-34

How to cite this URL:
Mahmood T, Yang PC. Western blot: Technique, theory, and trouble shooting. North Am J Med Sci [serial online] 2012 [cited 2020 Oct 30];4:429-34. Available from: https://www.najms.org/text.asp?2012/4/9/429/100998


  Introduction Top


Western blot is often used in research to separate and identify proteins. In this technique a mixture of proteins is separated based on molecular weight, and thus by type, through gel electrophoresis. These results are then transferred to a membrane producing a band for each protein. The membrane is then incubated with labels antibodies specific to the protein of interest.

The unbound antibody is washed off leaving only the bound antibody to the protein of interest. The bound antibodies are then detected by developing the film. As the antibodies only bind to the protein of interest, only one band should be visible. The thickness of the band corresponds to the amount of protein present; thus doing a standard can indicate the amount of protein present. The paper will first describe the protocol for western blot, accompanied by pictures to help the reader and theory to rationalize the protocol. This will be followed by the theoretical explanation of the procedure, and in the later section, troubleshooting tips for common problems.

Technique

Cell lysis to extract protein

Protein can be extracted from different kind of samples, such as tissue or cells. Below is the protocol to extract proteins from adherent cells.

Adherent cells:

  1. Wash cells in the tissue culture flask or dish by adding cold phosphate buffered saline (PBS) and rocking gently. Discard PBS. (Tip: Keep tissue culture dish on ice throughout).
  2. Add PBS and use a cell scraper to dislodge the cells. Pipette the mixture into microcentrifuge tubes.
  3. Centrifuge at 1500 RPM for 5 minutes and discard the supernatant.
  4. Add 180 μL of ice cold cell lysis buffer with 20 μL fresh protease inhibitor cocktail. (Tip: If protein concentration is not high enough at the end, it is advised to repeat the procedure with a higher proportion of protease inhibitor cocktail).
  5. Incubate for 30 minutes on ice, and then clarify the lysate by spinning for 10 minutes at 12,000 RPM, at 4°C.
  6. Transfer supernatant (or protein mix) to a fresh tube and store on ice or frozen at -20°C or -80°C.
  7. Measure the concentration of protein using a spectrophotometer.
Sample preparation



  1. determine the volume of protein extract to ensure 50 μg in each well.
  2. Add 5 μL sample buffer to the sample, and make the volume in each lane equalized using double distilled H 2 O (dd H 2 O). Mix well. (Tip: Total volume of 15 μL per lane is suggested).
  3. Heat the samples with dry plate for 5 minutes at 100°C.


Gel preparation



  1. After preparing the 10% stacking gel solution, assemble the rack for gel solidification [Figure 1]. (Tip: 10% AP and TEMED solidify the solution; therefore, both gels can be prepared at the same time, if the abovementioned reagents are not added until the end).
  2. Add stacking gel solution carefully until the level is equal to the green bar holding the glass plates [Figure 2]. Add H 2 O to the top. Wait for 15-30 minutes until the gel turning solidified. (Tip: Using a suction pipette can make the process of adding the gel to the glass plate easier).
  3. Overlay the stacking gel with the separating gel, after removing the water. (Tip: It is better to tilt the apparatus and use a paper towel to remove the water).
  4. Insert the comb, ensuring that there are no air bubbles.
  5. Wait until the gel is solidified. (Tip: Solidification can be easily checked by leaving some gel solution in a tube).
Figure 1: Assembled rack for gel solidification

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Figure 2: Add gel solution using a transfer pipette

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Electrophoresis

  1. Pour the running buffer into the electrophorator [Figure 3].
  2. Place gel inside the electrophorator and connect to a power supply. (Tip: When connecting to the power source always connect red to red, and black to black).
  3. Make sure buffer covers the gel completely, and remove the comb carefully.
  4. Load marker (6 μL) followed by samples (15 μL) in to each well [Figure 4].
  5. Run the gel with low voltage (60 V) for separating gel; use higher voltage (140 V) for stacking gel [Figure 5]a and b.
  6. Run the gel for approximately an hour, or until the dye front runs off the bottom of the gel [Figure 6].
Figure 3: Add running buffer to the electrophorator

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Figure 4: Add samples and molecular marker to the gel, after removing the combs

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Figure 5: (a) Samples running through the stacking gel (lower voltage). (b): Samples running through the separating gel (higher voltage)

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Figure 6: Run the gel to the bottom of the electrophorator

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Electrotransfer

  1. Cut 6 filter sheets to fit the measurement of the gel, and one polyvinylidene fluoride (PDVF) membrane with the same dimensions.
  2. Wet the sponge and filter paper in transfer buffer, and wet the PDVF membrane in methanol.
  3. Separate glass plates and retrieve the gel.
  4. Create a transfer sandwich as follows:

    Sponge

    3 Filter Papers

    Gel PVDF

    3 Filter Papers

    (Tip: Ensure there are no air bubbles between the gel and PVDF membrane, and squeeze out extra liquid).
  5. Relocate the sandwich to the transfer apparatus, which should be placed on ice to maintain 4°C. Add transfer buffer to the apparatus, and ensure that the sandwich is covered with the buffer. Place electrodes on top of the sandwich, ensuring that the PVDF membrane is between the gel and a positive electrode [Figure 7].
  6. Transfer for 90 minutes [Figure 8]. (Tip: The running time should be proportional to the thickness of the gel, so this may be reduced to 45 minutes for 0.75 mm gels).
Figure 7: Transfer should be done on ice

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Figure 8: Membrane after transfer

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Blocking and antibody incubation

  1. Block the membrane with 5% skim milk in TBST* for 1 hour.
  2. Add primary antibody in 5% bovine serum albumin ( BSA) and incubate overnight in 4°C on a shaker [Figure 9].
  3. Wash the membrane with TBST for 5 minutes. Do this 3 times. (Tip: All washing and antibody incubation steps should be done on a shaker at room temperature to ensure even agitation).
  4. Add secondary antibody in 5% skim milk in TBST, and incubate for 1 hour.
  5. Wash the membrane with TBST for 5 minutes. Do this 3 times
  6. Prepare ECL mix (following the proportion of solution A and B provided by the manufacturer). Incubate the membrane for 1-2 minutes [Figure 10]. (Tip: Use a 1000 μL pipette to ensure that ECL covers the top and bottom of the membrane).
  7. Visualize the result in the dark room [Figure 11]. (Tip: If the background is too strong, reduce exposure time).
*, TBST: Tris-Buffered Saline Tween-20
Figure 9: Use a shaker to incubate the membrane with antibody

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Figure 10: Incubate the membrane with ECL mix using a 1000 μL pipette to help the process

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Figure 11: Use the cassette to expose the membrane in the dark room

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Recipe

  1. Dissolve the following in 800 ml of distilled H 2 O

    • 8.8 g of NaCl
    • 0.2g of KCl
    • 3g of Tris base
  2. Add 500ul of Tween-20
  3. Adjust the pH to 7.4
  4. Add distilled H 2 O to 1L
  5. Sterilize by filtration or autoclaving
Theory

Sample preparation

Cell lysates are the most common form of sample used for western blot. Protein extraction attempts to collect all the proteins in the cell cytosol. This should be done in a cold temperature with protease inhibitors to prevent denaturing of the proteins. Since tissue sample display a higher degree of structure, mechanical invention, such as homogenization, or sonication is needed to extract the proteins.

After extracting the protein, it is very important to have a good idea of the extract's concentration. This eventually allows the researcher to ensure that the samples are being compared on an equivalent basis. Protein concentration is often measured using a spectrophotometer. Using this concentration allows to measure the mass of the protein that is being loaded into each well by the relationship between concentration, mass, and volume.

After determining the appropriate volume of the sample, it is diluted into a loading buffer, which contains glycerol so that the samples sink easily into the wells of the gel. A tracking dye (bromophenol blue) is also present in the buffer allowing the researcher to see how far the separation has progressed. The sample is heated after being diluted into a loading buffer, in order to denature the higher order structure, while retaining sulfide bridges. Denaturing the high structure ensures that the negative charge of amino acids is not neutralized, enabling the protein to move in an electric field (applied during electrotransfer).

It is also very important to have positive and negative controls for the sample. For a positive control a known source of target protein, such as purified protein or a control lysate is used. This helps to confirm the identity of the protein, and the activity of the antibody. A negative control is a null cell line, such as β-actin, is used as well to confirm that the staining is not nonspecific.

Gel electrophoresis

Western blot uses two different types of agarose gel: stacking and separating gel. The higher, stacking gel is slightly acidic (pH 6.8) and has a lower acrylamide concentration making a porous gel, which separates protein poorly but allows them to form thin, sharply defined bands. The lower gel, called the separating, or resolving gel, is basic (pH 8.8), and has a higher polyacrylamide content, making the gel's pores narrower. Protein is thus separated by their size more so in this gel, as the smaller proteins to travel more easily, and hence rapidly, than larger proteins.

The proteins when loaded on the gel have a negative charge, as they have been denatured by heating, and will travel toward the positive electrode when a voltage is applied. Gels are usually made by pouring them between two glass or plastic plates, using the solution described in the protocol section. The samples and a marker are loaded into the wells, and the empty wells are loaded with sample buffer. The gel is then connected to the power supply and allowed to run. The voltage is very important, as a high voltage can overheat and distort the bands.

Blotting

After separating the protein mixture, it is transferred to a membrane. The transfer is done using an electric field oriented perpendicular to the surface of the gel, causing proteins to move out of the gel and onto the membrane. The membrane is placed between the gel surface and the positive electrode in a sandwich. The sandwich includes a fiber pad (sponge) at each end, and filter papers to protect the gel and blotting membrane [Figure 12]. Here two things are very important: (1) the close contact of gel and membrane to ensure a clear image and (2) the placement of the membrane between the gel and the positive electrode. The membrane must be placed as such, so that the negatively charged proteins can migrate from the gel to the membrane. This type of transfer is called electrophoretic transfer, and can be done in semi-dry or wet conditions. Wet conditions are usually more reliable as it is less likely to dry out the gel, and is preferred for larger proteins.
Figure 12: Assembly of a sandwich in western Blot

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The membrane, the solid support, is an essential part of this process. There are two types of membrane: nitrocellulose and PVDF. Nitrocellulose is used for its high affinity for protein and its retention abilities. However, it is brittle, and does not allow the membrane to be used for reprobing. In this regard, PVDF membranes provide better mechanical support and allow the blot to be reprobed and stored. However, the background is higher in the PVDF membranes and therefore, washing carefully is very important.

Washing, blocking and antibody incubation

Blocking is a very important step of western blotting, as it prevents antibodies from binding to the membrane nonspecifically. Blocking is often made with 5% BSA or nonfat dried milk diluted in TBST to reduce the background.

Nonfat dried milk is often preferred as it is inexpensive and widely available. However, milk proteins are not compatible with all detection labels, so care must be taken to choose the appropriate blocking solution. For example, BSA blocking solutions are preferred with biotin and AP antibody labels, and antiphosphoprotein antibodies, since milk contains casein, which is itself a phosphoprotein and biotin, thus interfering with the assay results. It is often a good strategy to incubate the primary antibody with BSA since it is usually needed in higher amounts than the secondary antibody. Putting it in BSA solution allows the antibody to be reused, if the blot does not give good result.

The concentration of the antibody depends on the instruction by the manufacturer. The antibody can be diluted in a wash buffer, such as PBS or TBST. Washing is very important as it minimized background and removes unbound antibody. However, the membrane should not be left to wash for a really long time, as it can also reduce the signal.

The membrane is then detected using the label antibody, usually with an enzyme such as horseradish peroxidase (HRP), which is detected by the signal it produces corresponding to the position of the target protein. This signal is captured on a film which is usually developed in a dark room.

Quantification

It is very important to be aware that the data produced with a western blot is typically considered to be semi-quantitative. This is because it provides a relative comparison of protein levels, but not an absolute measure of quantity. There are two reasons for this; first, there are variations in loading and transfer rates between the samples in separate lanes which are different on separate blots. These differences will need to be standardized before a more precise comparison can be made. Second, the signal generated by detection is not linear across the concentration range of samples. Thus, since the signal produced is not linear, it should not be used to model the concentration.

Troubleshooting

Even though the procedure for western blot is simple, many problems can arise, leading to unexpected results. The problem can be grouped into five categories: (1) unusual or unexpected bands, (2) no bands, (3) faint bands or weak signal, (4) high background on the blot, and (5) patchy or uneven spots on the blot.

Unusual or unexpected bands can be due to protease degradation, which produces bands at unexpected positions. In this case it is advisable to use a fresh sample which had been kept on ice or alter the antibody. If the protein seems to be in too high of a position, then reheating the sample can help to break the quaternary protein structure. Similarly, blurry bands are often caused by high voltage or air bubbles present during transfer. In this case, it should be ensured that the gel is run at a lower voltage, and that the transfer sandwich is prepared properly. In addition, changing the running buffer can also help the problem. Nonflat bands can be the result of too fast of a travel through the gel, due to low resistance. To fix this the gel should be optimized to fit the sample. Finally, white (negative) bands on the film are due to too much protein or antibody.

Another problem: no bands can also arise due to many reasons related to antibody, antigen, or buffer used. If an improper antibody is used, either primary or secondary, the band will not show. In addition, the concentration of the antibody should be appropriate as well; if the concentration is too low, the signal may not be visible. It is important to remember that some antibodies are not to be used for western blot. Another reason for no visible bands is the lowest concentration or absence of the antigen. In this case, antigen from another source can be used to confirm whether the problem lies with the sample or with other elements, such as the antibody. Moreover, prolonged washing can also decrease the signal. Buffers can also contribute to the problem. It should be ensured that buffers like the transfer buffer, TBST, running buffer and ECL are all new and noncontaminated. If the buffers are contaminated with sodium azide, it can inactivate HRP.

Similarly, weak signals can be caused by low concentration of antibody or antigen. Increasing exposure time can also help to make the band clearer. Another reason could be nonfat dry milk masking the antigen. In this case use BSA or decrease the amount of milk used.

High background is often caused by too high concentration of the antibody, which can bind to PVDF membranes. Another problem could be the buffers, which may be too old. Increasing the washing time can also help to decrease the background. Additionally, too high of an exposure can also lead to this problem. Therefore, it is advisable to check different exposure times to achieve an optimum time.

Patchy and uneven spots on the blot are usually caused by improper transfer. If there are air bubbles trapped between the gel and the membrane, it will appear darker on the film. It is also important to use a shaker for all incubation, so that there is no uneven agitation during the incubation. Once again, washing is of utmost importance as well to wash the background. This problem can also be caused by antibodies binding to the blocking agents; in this case another blocking agent should be tried. Filtering the blocking agent can also help to remove some contaminants. Finally, this problem can also be caused by aggregation of the secondary antibody; in this case, the secondary antibody should be centrifuged and filtered to remove the aggregated.


  Conclusion Top


Western blot is a technique that is very useful for protein detection as it allows the user to quantify the protein expression as well. This paper covered the protocol, the theory behind that protocol, and some troubleshooting techniques. Western blot can be seen as an intricate balance, as the researcher attempts to get a nonspecific, yet strong signal.


    Figures

  [Figure 1], [Figure 2], [Figure 3], [Figure 4], [Figure 5], [Figure 6], [Figure 7], [Figure 8], [Figure 9], [Figure 10], [Figure 11], [Figure 12]


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84 Biomarkers of Multiple Sclerosis
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88 Complementarity of Matrix- and Nanostructure-Assisted Laser Desorption/Ionization Approaches
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97 EspA-loaded mesoporous silica nanoparticles can efficiently protect animal model against enterohaemorrhagic E. coli O157: H7
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99 An alternative pathway for the formation of aromatic aroma compounds derived from l -phenylalanine via phenylpyruvic acid in tea ( Camellia sinensis (L.) O. Kuntze) leaves
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104 Aspalathin-Enriched Green Rooibos Extract Reduces Hepatic Insulin Resistance by Modulating PI3K/AKT and AMPK Pathways
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122 Oxidative Stress-Protective and Anti-Melanogenic Effects of Loliolide and Ethanol Extract from Fresh Water Green Algae, Prasiola japonica
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125 Divergent changes in the content and activity of MMP-26 and TIMP-4 in human umbilical cord tissues associated with preeclampsia
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128 Evaluation methods as quality control in the generation of decellularized peripheral nerve allografts
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132 Comparison of untagged and his-tagged dihydrodipicolinate synthase from the enteric pathogen Vibrio cholerae
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133 Expression, activation and processing of a novel plant milk-clotting aspartic protease in Pichia pastoris
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134 Zinc stimulates glucose oxidation and glycemic control by modulating the insulin signaling pathway in human and mouse skeletal muscle cell lines
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135 Assessment of TSPO in a Rat Experimental Autoimmune Myocarditis Model: A Comparison Study between [18F]Fluoromethyl-PBR28 and [18F]CB251
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136 Effect of TAK1 on osteogenic differentiation of mesenchymal stem cells by regulating BMP-2 via Wnt/ß-catenin and MAPK pathway
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137 Identification of protective protein antigens for vaccination against Streptococcus dysgalactiae in cobia ( Rachycentron canadum )
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138 Plasmonic biosensor based on vertical arrays of gold nanoantennas
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139 The protective mechanism of Nigella sativa against diethylnitrosamine-induced hepatocellular carcinoma through its antioxidant effect and EGFR/ERK1/2 signaling
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140 Photodynamic inactivation of bacteriophage MS2: The A-protein is the target of virus inactivation
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141 Involvement of a Nonstructural Protein in Poliovirus Capsid Assembly
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142 Identification of a novel member of the pH responsive pathway Pal/Rim in Ustilago maydis
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143 ??????????????? ???????? ??????????????? ??????????????? ????????????? ??????? ??? ?????? ??? ???????? ?????? ?????????????? ????????, "?????????"
?. ?. ???,?.?. ????????,?. ?. ????????,?.?. ?????????,?.?. ??????
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144 A Proteomics and other Omics approach in the context of farmed fish welfare and biomarker discovery
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145 The role of posttranslational modifications of a-synuclein and LRRK2 in Parkinsonæs disease: Potential contributions of environmental factors
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146 Nitroso-Oxidative Stress, Acute Phase Response, and Cytogenetic Damage in Wistar Rats Treated with Adrenaline
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147 Padlock Probe Assay for Detection and Subtyping of Seasonal Influenza
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148 Microchannel device for proteomic analysis of migrating cancer cells
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149 Role of Dehydrin-FK506-binding proteins complex in enhancing drought tolerance through ABA-mediated signaling pathway
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150 Ameliorative role of ferulic acid against diabetes associated oxidative stress induced spleen damage
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151 5-Methoxyindole-2-carboxylic acid (MICA) suppresses Aß-mediated pathology in C. elegans
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152 Early Diagnosis of Disease Using Microbead Array Technology: A Review
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153 Polydopamine/Transferrin Hybrid Nanoparticles for Targeted Cell-Killing
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154 Cryoablation inhibition of distant untreated tumors (abscopal effect) is immune mediated
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155 Differential antiviral activity of European sea bass interferon-stimulated 15 protein (ISG15) against RGNNV and SJNNV betanodaviruses
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156 An ice-binding and tandem beta-sandwich domain-containing protein in Shewanella frigidimarina is a potential new type of ice adhesin
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157 A non-canonical GTPase interaction enables ORP1L-Rab7-RILP complex formation and late endosome positioning
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158 Highly Sensitive and Multiplexed Protein Measurements
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159 5-hydroxytryptamine1A receptor density in the hippocampus of patients with temporal lobe epilepsy is associated with disease duration
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160 High concentration of trichlorfon (1mM) disrupts axonal cytoskeleton and decreases the expression of plasticity-related proteins in SH-SY5Y cells
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161 Immunomodulatory and therapeutic role of Cinnamomum verum extracts in collagen-induced arthritic BALB/c mice
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162 Altered functional efficacy of hippocampal interneuron during epileptogenesis following febrile seizures
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163 Hypoglycemic and anti-inflammatory effects of Psacalium paucicapitatum corms infusions
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164 Proteomics and irritable bowel syndrome
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165 A novel mouse model of anterior segment dysgenesis (ASD): conditional deletion ofTsc1disrupts ciliary body and iris development
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166 Toxin-Antitoxin Systems in Estuarine Synechococcus Strain CB0101 and Their Transcriptomic Responses to Environmental Stressors
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167 Fruit Peel Polyphenolic Extract-Induced Apoptosis in Human Breast Cancer Cells Is Associated with ROS Production and Modulation of p38MAPK/Erk1/2 and the Akt Signaling Pathway
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168 Quantitative proteome-based systematic identification of SIRT7 substrates
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169 The ENU-3 protein family members function in the Wnt pathway parallel to UNC-6/Netrin to promote motor neuron axon outgrowth in C. elegans
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170 Cigarette smokers develop altered erythrocyte membrane composition: an investigation unmasking the role of membrane bound integral protein GLUT 1
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171 Development and application of an enzyme-linked immunosorbent assay (ELISA) using a soluble recombinant nucleoprotein for the detection of antibodies to avian influenza virus
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172 Processing fixed and stored adipose-derived stem cells for quantitative protein array assays
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173 Short-term regular aerobic exercise reduces oxidative stress produced by acute high intraluminal pressure in the adipose microvasculature
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174 Combining Cytotoxicity Assessment and Xenopus laevis Phenotypic Abnormality Assay as a Predictor of Nanomaterial Safety
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175 DNA polymerase beta participates in DNA End-joining
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176 Expression of Aspergillus Niger N5-5 in E. coli and Purification and Identification of Products
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177 Attenuation of the Infiltration of Angiotensin II Expressing CD3+ T-Cells and the Modulation of Nerve Growth Factor in Lumbar Dorsal Root Ganglia – A Possible Mechanism Underpinning Analgesia Produced by EMA300, An Angiotensin II Type 2 (AT2) Receptor Antagonist
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179 Protective Effects of ?-Mangostin on 6-OHDA-Induced Toxicity in SH-SY5Y Cells
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180 Using SDS-PAGE gel fingerprinting to identify soft-bodied wood-boring insect larvae to species
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181 Human Sirtuin 3 (SIRT3) deacetylates histone H3 lysine 56 to promote Nonhomologous end joining repair
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182 Telmisartan Activates PPARd to Improve Symptoms of Unpredictable Chronic Mild Stress-Induced Depression in Mice
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183 Deoxycholic acid promotes development of gastroesophageal reflux disease and Barrettæs oesophagus by modulating integrin-av trafficking
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184 Intracranial self-stimulation and immobilization had different effects on neurite extension and the p38 MAPK pathway in PC12m3 cells
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186 Bloch Surface Waves Biosensors for High Sensitivity Detection of Soluble ERBB2 in a Complex Biological Environment
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187 Inhibition of heat shock protein (Hsp) 90 potentiates the antiproliferative and pro-apoptotic effects of 2-(4'fluoro-phenylamino)-4H-1,3-thiazine[6,5-b]indole in A2780cis cells
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188 A Novel Egr-1-Agrin Pathway and Potential Implications for Regulation of Synaptic Physiology and Homeostasis at the Neuromuscular Junction
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189 Autophagy enhancement is rendered ineffective in presence of a-synuclein in melanoma cells
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190 Semi-Automatic Analysis for Unidimensional Immunoblot Images to Discriminate Breast Cancer Cases Using Time Series Data Mining
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191 TNF-a exerts cytotoxic effects on multidrug resistant breast cancer MCF-7/MX cells via a non-apoptotic death pathway
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192 Capsanthin Inhibits both Adipogenesis in 3T3-L1 Preadipocytes and Weight Gain in High-Fat Diet-Induced Obese Mice
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195 Affinity Pulldown of Biotinylated RNA for Detection of Protein-RNA Complexes
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196 3D tumor spheroids: an overview on the tools and techniques used for their analysis
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199 Easy and Fast Western Blotting by Thin-Film Direct Coating with Suction
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200 Influence of Clinically Relevant Mechanical Forces on Vascular Smooth Muscle Cells Under Chronic High Glucose: An In Vitro Dynamic Disease Model
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201 Neuroprotective Effect of Puerarin on Glutamate-Induced Cytotoxicity in Differentiated Y-79 Cells via Inhibition of ROS Generation and Ca2+ Influx
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