Monoclonal Anti-Phosphoserine−Biotin antibody produced in mouse

Monoclonal Anti-Phosphoserine (mouse IgG1 isotype) is derived from the PSR-45 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice.

Reversible phosphorylation of proteins is an important post-translational modification that plays a regulatory role in the expression of most proteins in the cells. Reversible phosphorylation at multiple serine, tyrosine and threonine residues mediate numerous signalling pathways in both prokaryotic and Eukaryotic cells. Cellular proteins with phosphorylated serine increase many fold by the activation of serine kinases. Most mitogenic receptor systems such as EGF, PDGF, insulin receptors contain serine/threonine/tyrosine kinase domains that undergo autophosphorylation when receptors bind to the respective ligands. T cell antigen receptor complex or the receptors for some hemopoietic growth factors may stimulate these phosphorylation associated kinases, and cells transformed by viral oncogenes contain elevated levels of phosphorylated tyr/ser/thr.
Monoclonal Anti-Phosphoserine may be used for the identification of proteins containing phosphorylated serine both as the free amino acid or when conjugated to carriers such as BSA or KLH. The purified mouse immunoglobulin from ascites fluid is conjugated to biotinamidohexanoic acid N-hydroxysuccinimide ester. This covalent coupling of biotin to the immunoglobulin allows for the binding of avidin or streptavidin bearing a variety of different labels.

phosphoserine conjugated to Keyhole Limpet Hemocyanin (KLH).

Monoclonal Anti-Phosphoserine-Biotin antibody produced in mouse has been used in western blotting.

Monoclonal Anti-Phosphoserine−Biotin antibody may be used in indirect ELISA at a recommended dilution of 1:50,000 - 1:100,000. The antibody may be used for detection by dot blot at a working dilution of 1:200,000.

By ELISA and dot blot, the antibody reacts specifically with phosphorylated serine, both as free amino acid or conjugated to carriers such as BSA or KLH. No cross-reactivity is observed with non-phosphorylated serine, phosphothreonine, phosphotyrosine, AMP or ATP. This antibody has been used in immunoblotting for the localization of some phosphoserine-containing proteins. Certain proteins known to contain phosphorylated serine may not be recognized by this antibody due to steric hindrance of the recognition site.

Solution in phosphate buffered saline containing 1% bovine serum albumin and 15 mM sodium azide.

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