亚美尼亚仓鼠单克隆抗体[HM beta 3.1] to Integrin beta 3 (FITC)
FITC. Ex: 493nm, Em: 528nm
Recognises 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.
Shipped 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.
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.
Isoform 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.
Defects 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.
Belongs to the integrin beta chain family. Contains 1 VWFA domain.
Phosphorylated 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.