This antibody detects integrin beta-3 tyrosine phosphorylation both in vitro and in platelets by specifically recognizing phosphorylated Tyr759 on the beta-3 cytoplasmic domain and can be useful for understanding specific cell signaling mechanisms more clearly.
Integrin beta3, also known as CD61, is a 130 kDa transmembrane glycoprotein that binds noncovalently in complexes with integrin alpha subunits to form the functional receptor that binds to specific extracellular matrix proteins (e.g., fibronectin, vitronectin, etc.). Integrin receptors are involved in the regulation of a variety of important biological functions, including embryonic development, wound repair, hemostasis, and prevention of programmed cell death. They are also implicated in abnormal pathological states such as tumor directed angiogenesis, tumor cell growth, and metastasis.
From the laboratory of Xiaoping Du, MD, PhD, University of Illinois at Chicago.
Part of The Investigator's Annexe program.
|Antigen:||Phosphorylated Y759 of B3 integrin|
|Immunogen:||B3 integrin peptide linked to KLH: KLH-CTpYRGT|
|Purification Method:||Absorbed three times with Sepharose 4B coupled with a non-phosphorylated CTYRGT peptide to remove phosphorylation-independent reactivity|
|Tested Applications:||WB, IF, IHC|
The effect of tyrosine phosphorylation on calpain cleavage of synthetic beta3 cytoplasmic domain peptides.
(A) The integrin beta3 cytoplasmic domain peptide sequence with tyrosine phosphorylation and calpain cleavage sites indicated. (B) Synthetic peptides corresponding to beta3 cytoplasmic domain with (beta3CpY) or without (beta3C) phosphorylation at Tyr759 were incubated with purified µ-calpain at 30C for 30 min and analyzed by SDS-PAGE and Western blotting with Ab pY759, a phosphotyrosine-specific anti-beta3 antibody. Adapted from: Xi X, Flevaris P, Stojanovic A, Chishti A, Phillips DR, Lam SC, and Du X. Tyrosine phosphorylation of the integrin beta 3 subunit regulates beta 3 cleavage by calpain.Journal of Biological Chemistry. 281(40):29426-29430, 2006.
Beta3 tyrosine phosphorylation and calpain cleavage in platelets spreading on fibrinogen.
Platelets were allowed to spread on fibrinogen-coated slides for 90 min, fixed, and permeabilized. The slides were stained with a mouse anti-beta3 extracellular domain antibody, mAb15 (green) and the tyrosine phosphorylation-specific (pY759) anti-beta3 antibody (red). Affinity-depleted Ab 759 antiserum was used as negative control (NC). Data were collected with a Zeiss confocal microscope (63× lens).Adapted from: Xi X, Flevaris P, Stojanovic A, Chishti A, Phillips DR, Lam SC, and Du X. Tyrosine phosphorylation of the integrin beta 3 subunit regulates beta 3 cleavage by calpain.Journal of Biological Chemistry. 281(40):29426-29430, 2006.
If you publish research with this product, please let us know so we can cite your paper.