By John R. Gordon
Read or Download A Practical Guide to Cellular and Molecular Research Methods in Immunology, 2nd Edition PDF
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Extra resources for A Practical Guide to Cellular and Molecular Research Methods in Immunology, 2nd Edition
Example text
However, it is an ideal method to confirm the homogeneity or lack thereof of purified proteins. 006% Coomassie Brilliant Blue G-250 in 10% glacial acetic acid) protein samples biotinylated molecular weight markers (for Western blots) unstained molecular weight markers (for protein staining gels) METHOD 1. Clean the glass plates and gaskets, and assemble the PAGE apparatus. Place a mark on the glass at the 6 cm mark (from the bottom). 2. 2 ml of H2O. Degas the solution under vacuum for 10 - 15 min.
A. Bio-Rad, Bradford or CBB] protein assay; Appendix D), and pool the protein-containing fractions. Regenerate the column with ≈10 ml of PBS, and store the matrix in PBS/20% ethanol. ). After dialysis, determine the protein concentration of the eluted IgG solution using a and, if necessary, concentrate the eluted protein using a centrifugal concentrator. , protein A, T gel, Avid-Chrom), so alternate methods must be employed to prepare IgM antibodies. A number of methods are available, with the simplest true purification probably being achieved by size exclusion chromatography (IgM pentamers have a molecular mass of ≈750 kD, while IgG and albumin have molecular masses of 150 & 65 kD, respectively).
Cover and incubate at room temperature for ≈90 min. 5. Wash the wells 8 - 10 times with PBST, and add 100 µl of the diluted SA-HRP (1:5000) to each well. Incubate at room temperature for ≈90 min. 6. Wash the plates 8 - 10 times with distilled H2O, making sure to remove excess fluid. Add 100 µl of ABTS substrate to each well and allow the reactions to develop for 20 - 45 min at room temperature. The reactions can be stopped by 7. adding 100 µl of 1% SDS to each well. Read the plates using the ELISA plate reader, set at a reading wavelength of 405 nm.