We all know the famous affinity tables of Protein A and G binding to different IgGs of several species. In fact, mouse IgG1 is known to bind (very) poorly to Protein A but posses a strong affinity for Protein G. However, when reading publications in which they employ a specific IP with Mouse IgG1 researchers are still very often using Protein A.
Why is this? Am I missing something?
I am asking this because I have some very bad results when immunoprecipitating with an anti-Albumin Mouse IgG1 antibody in HepG2 (human) cell lysates employing Protein G beads. Researchers have found succes though employing Protein A beads but it did not make any sense at all.
Thank you in advance!
Hi William,
You may check https://www.neb.com/tools-and-resources/selection-charts/affinity-of-protein-ag-for-igg-types-from-different-species
Dear Rana,
Thank you for your answer. As I citate from my question, I describe the table.. "..We all know the famous affinity tables of Protein A and G binding to different IgGs of several species. In fact, mouse IgG1 is known to bind (very) poorly to Protein A but posses a strong affinity for Protein G..."
Therefore my question is not about reading the table itself; its why people use Protein A beads when employing mouse IgG1 antibodies in immunoprecipitation? Their affinity is poor and it makes absolutely no sense to me.
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