Brand : ECM Biosciences
Phosphorylation of specific serine or threonine residues is an important post-translational modification for regulating the activity of most proteins. Stimulation of a variety of cell signaling pathways activates the receptor and non-receptor ser/thr kinases that mediate these protein modifications. Antibodies that can detect phosphoserine or phosphothreonine residues are excellent tools for characterizing changes in the post-translational state of a broad range of phosphorylated proteins. Immunoprecipitation of proteins of interest followed by detection of phosphoserine or phosphothreonine using anti-phosphoserine antibody is commonly used to correlate changes in phosphorylation state with alterations in protein activity.
Western blot analysis of A431 cells treated with calyculin A (100 nM) for 30 min (lane 1) then treated with lambda phosphatase (lane 2). The blot was probed with anti-Phosphoserine/threonine rabbit polyclonal at 1:1000.
Bar graph showing anti-Phosphoserine/threonine (PP2551) binding to a variety of phosphoserine and phosphothreonine peptides, but not control peptide containing unphosphorylated serine or phosphotyrosine.
WB, E, IP, ICC
Rabbit polyclonal, affinity-purified antibody is supplied in 100μl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
The products are are safely shipped at ambient temperature for both domestic and international shipments. Each product is guaranteed to match the specifications as indicated on the corresponding technical data sheet. Please store at -20C upon arrival for long term storage.
This antibody was cross-adsorbed to unphosphorylated peptide then affinity purified using a mix of phosphoserine and phosphothreonine peptides (without carrier). The antibody detects many serine or threonine phosphorylated proteins by western blot, immunocytochemistry, and ELISA.