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GP9 encodes a small membrane glycoprotein found on the surface of human platelets. Additionally we are shipping CD42a Proteins (11) and CD42a Kits (3) and many more products for this protein.
Showing 10 out of 106 products:
Human Monoclonal CD42a Primary Antibody for FACS - ABIN1981875
Din, Aftab, Jubb, Carnegy, Lyall, Sarma, Newby, Flapan: Effect of moderate walnut consumption on lipid profile, arterial stiffness and platelet activation in humans. in European journal of clinical nutrition 2011
Show all 3 references for ABIN1981875
Human Monoclonal CD42a Primary Antibody for FACS - ABIN118641
Sarma, Laan, Alam, Jha, Fox, Dransfield: Increased platelet binding to circulating monocytes in acute coronary syndromes. in Circulation 2002
Human Monoclonal CD42a Primary Antibody for FACS, IHC (fro) - ABIN119462
Zola, McNamara, Beckman, Brooks, Macardle, Bradley, Goodall, Skinner, Collins, Berndt: Monoclonal antibodies against antigens of the human platelet surface: preparation and properties. in Pathology 1984
A Lyn (show LYN Antibodies)-Vav (show VAV1 Antibodies)-Rac1-PI3K-Akt (show AKT1 Antibodies) pathway mediates von Willebrand factor (show VWF Antibodies)-induced activation of integrin alpha(IIb (show ITGA2B Antibodies))beta(3) to promote GPIb-IX-dependent platelet activation.
Data indicate that GPIX is the subunit of the glycoprotein Ib-IX-V complex that binds to grp94/Hsp90b1 (show HSP90B1 Antibodies); the glycoprotein Ib-IX-V complex is stabilized by grp94/Hsp90b1 (show HSP90B1 Antibodies).
factor XI is localized to GPIb in membrane rafts and this association is important for promoting the activation of factor XI by thrombin (show F2 Antibodies) on the platelet surface
Data show that localization of the GP Ib-IX complex to the lipid domain is mediated by GP Ibbeta and GP IX transmembrane domains.
genetic association study in population in western India: Data suggest novel mutations in platelet glycoprotein Ib (GP1BA (show GP1BA Antibodies), GP1BB (show GP1BB Antibodies)) and GP9 are associated with Bernard-Soulier syndrome in subjects studies; of 12 mutations identified, ten were novel.
Studies indicate that platelets from Bernard-Soulier syndrome (BSS (show GP1BA Antibodies)) are defective in glycoprotein (GP)Ib-IX-V, a platelet-specific adhesion-signaling complex, composed of GPIbalpha (show GP1BA Antibodies) disulfide linked to GPIbbeta, and noncovalently associated with GPIX and GPV (show GP5 Antibodies).
GPIX increased the expression of GPIba (show GP1BA Antibodies) by promoting the formation of a disulfide bond between GPIba (show GP1BA Antibodies) and GPIbb (show GP1BB Antibodies) in transfected CHO (show COL11A1 Antibodies)-K1 cells.
GPIbbeta missense mutations from Bernard-Soulier syndrome were examined for changes to GPIb-IX complex surface expression. Mutations A108P and P74R were found to maintain normal secretion/folding of GPIbbeta(E) but were unable to support GPIX surface expression
GPIIb (show ITGA2B Antibodies)/IIIa is the primary receptor set involved in platelet adhesion to adsorbed fibrinogen and serum albumin (show ALB Antibodies) irrespective of their degree of adsorption-induced unfolding, while the GPIb-IX-V receptor complex plays an insignificant role.
GP Ibbeta/GP IX mediates the disulfide-linked GP Ibalpha localization to the GEMs, which is critical for vWf (show VWF Antibodies) interaction at high shear
14-3-3beta, 14-3-3gamma, 14-3-3epsilon, 14-3-3eta and 14-3-3theta isoforms interact with the GPIb-IX complex in platelets
the putative convex surface of the LRR domain in GPIX is sufficient, in the context of full-length subunit, to mediate its association with GPIbbeta
This gene encodes a small membrane glycoprotein found on the surface of human platelets. It forms a 1-to-1 noncovalent complex with glycoprotein Ib, a platelet surface membrane glycoprotein complex that functions as a receptor for von Willebrand factor. The complete receptor complex includes noncovalent association of the alpha and beta subunits with the protein encoded by this gene and platelet glycoprotein V. Defects in this gene are a cause of Bernard-Soulier syndrome, also known as giant platelet disease. These patients have unusually large platelets and have a clinical bleeding tendency.
glycoprotein IX (platelet)
, glycoprotein 9 (platelet)
, platelet glycoprotein IX
, glycoprotein 9