Detection of Integrin alpha V beta 3 in HUVEC Human Cells by Flow Cytometry.
HUVEC human umbilical vein endothelial cells were stained with Mouse Anti-Human Integrin alpha V beta 3 PE‑conjugated Monoclonal Antibody (Catalog # FAB3050P, filled histogram) or isotype control antibody (Catalog # IC002P, open histogram). View our protocol for Staining Membrane-associated Proteins.
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze.
12 months from date of receipt, 2 to 8 °C as supplied.
Background: Integrin alpha V beta 3
Integrin alpha V beta 3, together with Integrin alpha IIb beta 3, constitute the only known beta 3 Integrins (1‑3). The non-covalent heterodimer of 170 kDa alpha V/CD51 and 93 kDa beta 3/CD61 subunits shows wide expression, notably by endothelial cells and osteoclasts (2‑4). Each subunit has a transmembrane sequence and a short cytoplasmic tail connected to the cytoskeleton. Active cell surface alpha V beta 3 adheres to matrix proteins including vitronectin, fibronectin, fibrinogen and thrombospondin (2, 3). The ligand binding site of alpha V beta 3 is in the N-terminal head region, formed by interaction of the beta 3 vWFA domain with the alpha V beta-propeller structure (4). The alpha V subunit contributes a thigh and a calf region, while the beta 3 subunit contains a PSI domain and four cysteine-rich I-EGF folds. The alpha V subunit domains termed thigh, calf-1 and calf-2 generate a “knee” region that is bent when the alpha V beta 3 is in its constitutively inactive state. Activation, either by “inside out” signaling or by Mg2+ or Mn2+ binding, extends the Integrin to expose its ligand binding site (1, 4). Two splice variants of beta 3 (b and c) diverge over the last 21 amino acids (aa) and lack cytoplasmic phosphorylation sites (5, 6). Another beta 3 splice variant diverges after the vWFA domain, producing a soluble 60 kDa form in platelets and endothelial cells (7). alpha V beta 3 is essential for the maturation of osteoclasts and their binding and resorption of bone; it also, however, promotes their apoptosis (8, 9). M-CSF R and alpha V beta 3 share signaling pathways during osteoclastogenesis, and deletion of either molecule causes osteopetrosis (8, 9). Also cell entry of several viruses is mediated by alpha V beta 3 (4, 10). The 962 aa human alpha V ECD (11) shares 92‑95% aa sequence identity with mouse, rat and cow alpha V while the 685 aa human beta 3 ECD (12) shares 95% aa identity with horse and dog, and 89‑92% aa identity with mouse, rat and pig beta 3.
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Entrez Gene IDs:
antigen identified by monoclonal L230; CD51 antigen; CD51; Integrin alpha V beta 3; integrin alpha-V; integrin, alpha V (vitronectin receptor, alpha polypeptide, antigen CD51); MSK8; Vitronectin receptor subunit alpha; VNRADKFZp686A08142
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