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Western blot analysis of Integrin β3 on a human platelet lysate. Lane 1: 1:2500, lane 2: 1:5000, lane 3: 1:10000 dilution of the anti- human CD61 antibody.
BD Transduction Laboratories™ Purified Mouse Anti-Human CD61
Regulatory Statusの凡例
Any use of products other than the permitted use without the express written authorization of Becton, Dickinson and Company is strictly prohibited.
Preparation and Storage
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
関連製品
Integrins are heterodimeric transmembrane receptors that mediate cell-cell or cell-matrix adhesion. They contain noncovalently associated α and β subunits that consist of a large extracellular region (the ligand-binding domain), a short transmembrane region, and a cytoplasmic domain of varying length. In mammals, at least 17 α subunits and 8 β subunits have been identified and these proteins can heterodimerize to form at least 22 different receptors. Although there is a high degree of redunancy, each integrin has a specific biological function. For example, the β3 subunit associates with αIIb in platelets where this glycoprotein complex acts as a fibrinogen receptor and mediates platelet aggregation. In endothelial cells (EC), β3 complexes with the αv subunit to form the vitronectin receptor. This receptor mediates endothelial cell adhesion to vitronectin, fibrinogen, von Willebrand factor, thrombospondin, laminin, and fibronectin. In confluent EC cultures, the αvβ3 integrin localizes to focal adhesions at the cell body and cell-cell borders. Thus, continued study of individual integrin subunits will provide insights to mechanisms of cell adhesion and signaling.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.
Development References (5)
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Albelda SM, Daise M, Levine EM, Buck CA. Identification and characterization of cell-substratum adhesion receptors on cultured human endothelial cells. J Clin Invest. 1989; 83(6):1192-2002. (Biology). View Reference
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Chen YP, Djaffar I, Pidard D, et al. Ser-752-->Pro mutation in the cytoplasmic domain of integrin beta 3 subunit and defective activation of platelet integrin alpha IIb beta 3 (glycoprotein IIb-IIIa) in a variant of Glanzmann thrombasthenia. Proc Natl Acad Sci U S A. 1992; 89(21):10169-10173. (Biology). View Reference
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Greenwood JA, Theibert AB, Prestwich GD, Murphy-Ullrich JE. Restructuring of focal adhesion plaques by PI 3-kinase. Regulation by PtdIns (3,4,5)-p(3) binding to alpha-actinin. J Cell Biol. 2000; 150(3):627-642. (Biology: Immunoprecipitation). View Reference
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Tang S, Gao Y, Ware JA. Enhancement of endothelial cell migration and in vitro tube formation by TAP20, a novel beta 5 integrin-modulating, PKC theta-dependent protein. J Cell Biol. 1999; 147(5):1073-1084. (Biology: Western blot). View Reference
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Yip KP, Marsh DJ. An Arg-Gly-Asp peptide stimulates constriction in rat afferent arteriole. Am J Physiol. 1997; 273(5):F768-F776. (Biology: Immunohistochemistry). View Reference
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Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
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