Recombinant intracellular fragment (aa 97-432) of human Cbp (PAG).
PAG (phosphoprotein associated with GEMs), also known as Cbp (Csk-binding protein), is a ubiquitously expressed 46 kDa transmembrane adaptor protein present in membrane rafts (glycosphingolipid-enriched microdomains), which however migrates on SDS PAGE gels anomalously as an 80 kDa molecule. Following tyrosine phosphorylation by Src family kinases, PAG binds and thereby activates the protein tyrosine kinase Csk, the major negative regulator of the Src family kinases. Signaling via the B-cell receptor in B cells or high affinity IgE receptor (FcepsilonRI) in mast cells leads to PAG increased tyrosine phosphorylation and Csk binding, while T cell receptor signaling causes PAG dephosphorylation, loss of Csk binding and increased activation of the protein tyrosine kinase Lck.
Clonality:
Monoclonal
Concentration:
1 mg/ml
Clone Designation:
[PAb 409]
Isotype:
Rabbit polyclonal
Buffer:
Phosphate buffered saline (PBS), pH 7.4, 15 mM sodium azide
