Armenian Hamster monoclonal [HM beta 3.1] to Integrin beta 3 (FITC)
ConjugationFITC. Ex: 493nm, Em: 528nm
SpecificityRecognises the murine integrin beta 3 subunit (CD61), a 90kD a type I membrane protein, which is expressed primarily on megakaryocytes, platelets, monocytes, macrophages, granulocytes and endothelial cells. CD61 associates with either the alpha IIb integrin (CD41) or the alpha V integrin (CD51) to form the platelet glycoprotein complex IIb/IIIa and the vitronectin receptor (VNR) respectively. The heterodimers formed with CD61 are receptors for a variety of ligands including fibrinogen, fibronectin, von Willebrands factor (vWF), vitronectin and thrombospondin.
Tissue, cells or virus corresponding to Mouse Integrin beta 3. Mouse integrin alpha 5 beta 3 protein purified from the mouse hybridoma 2B4. Database link: O54890
Recognizes the murine integrin beta 3 subunit (CD61), a 90kD a type I membrane protein, which is expressed primarily on megakaryocytes, platelets, monocytes, macrophages, granulocytes and endothelial cells. CD61 associates with either the alpha IIb integrin (CD41) or the alpha V integrin (CD51) to form the platelet glycoprotein complex IIb/IIIa and the vitronectin receptor (VNR) respectively. The heterodimers formed with CD61 are receptors for a variety of ligands including fibrinogen, fibronectin, von Willebrand's factor (vWF), vitronectin and thrombospondin.
Clone HM beta 3.1 is reported to partially inhibit the binding of CD61 to fibronectin.
Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at +4°C. Store In the Dark.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/10. ab18473-Armenian Hamster monoclonal IgG, is suitable for use as an isotype control with this antibody.
FunctionIntegrin 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.
Tissue specificityIsoform beta-3A and isoform beta-3C are widely expressed. Isoform beta-3A is specifically expressed in osteoblast cells; isoform beta-3C is specifically expressed in prostate and testis.
Involvement in diseaseDefects in ITGB3 are a cause of Glanzmann thrombasthenia (GT) [MIM:273800]; also known as thrombasthenia of Glanzmann and Naegeli. GT is the most common inherited disease of platelets. It is an autosomal recessive disorder characterized by mucocutaneous bleeding of mild-to-moderate severity and the inability of this integrin to recognize macromolecular or synthetic peptide ligands. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb/beta-3 complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the glycoprotein IIb/beta-3 complex at reduced levels (5-20% controls), have detectable amounts of fibrinogen, and have low or moderate clot retraction capability. The platelets of GT 'variants' have normal or near normal (60-100%) expression of dysfunctional receptors.
Sequence similaritiesBelongs to the integrin beta chain family. Contains 1 VWFA domain.
Post-translational modificationsPhosphorylated on tyrosine residues in response to thrombin-induced platelet aggregation. Probably involved in outside-in signaling. A peptide (AA 740-762) is capable of binding GRB2 only when both Tyr-773 and Tyr-785 are phosphorylated. Phosphorylation of Thr-779 inhibits SHC binding.