Description
Integrin beta3 (phospho Tyr785) Antibody | 79-490 | Gentaur UK, US & Europe Distribution
Host: Rabbit
Reactivity: Human, Mouse
Homology: N/A
Immunogen: Integrin beta3 (Phospho-Tyr785) antibody was raised against a peptide sequence around phosphorylation site of tyrosine 785 (I-T-Y (p) -R-G) derived from Human Integrin β3.
Research Area: Phospho-Specific
Tested Application: WB
Application: Western Blot: 1:500~1:1000
Specificiy: This antibody detects endogenous level of Integrin β3 only when phosphorylated at tyrosine 785.
Positive Control 1: N/A
Positive Control 2: N/A
Positive Control 3: N/A
Positive Control 4: N/A
Positive Control 5: N/A
Positive Control 6: N/A
Molecular Weight: 110 kDa
Validation: N/A
Isoform: N/A
Purification: Antibodies were purified by affinity-chromatography using epitope-specific phosphopeptide. Non-phospho specific antibodies were removed by chromatogramphy using non-phosphopeptide.
Clonality: Polyclonal
Clone: N/A
Isotype: N/A
Conjugate: Unconjugated
Physical State: Liquid
Buffer: Antibody supplied in phosphate buffered saline (without Mg2+ and Ca2+) , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Concentration: 1 mg/mL
Storage Condition: Store antibody at -20˚C for up to one year.
Alternate Name: GT, CD61, GP3A, BDPLT2, GPIIIa, BDPLT16, RAF, CD61 antigen, ITB3, Platelet membrane glycoprotein IIIa
User Note: N/A
BACKGROUND: Integrin alpha-V/beta-3 is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. Integrins alpha-IIb/beta-3 and alpha-V/beta-3 recognize the sequence R-G-D in a wide array of ligands. Integrin alpha-IIb/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial surface. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.