Overview
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.
Specificity:
The antibody MEM-255 recognizes an epitope (aa 235-280) of Csk-binding protein (Cbp) located in the cytoplasmic domain, also known as protein associated with glycosphingolipid-enriched microdomains (PAG) .
Antigen
PAG1
Clone
MEM-255
Species Reactivity
Human
Negative Species
Mouse, Rat, Cow
Isotype
Mouse IgG2a
Immunogen
Recombinant intracellular fragment (aa 97-432) of human Cbp (PAG) .
Application
WB, IHC (P), FC (IC)
Regulatory status
RUO
Concentration
1 mg/ml
Format
Purified
Storage / Stability
Store at 2-8°C. Do not freeze.
Storage Buffer
Phosphate buffered saline (PBS), pH 7.4, 15 mM sodium azide