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GP9 encodes a small membrane glycoprotein found on the surface of human platelets. Additionally we are shipping CD42a Antibodies (109) and CD42a Proteins (12) and many more products for this protein.
Showing 10 out of 19 products:
A Lyn-Vav-Rac1-PI3K-Akt pathway mediates von Willebrand factor-induced activation of integrin alpha(IIb)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 ELISA Kits); the glycoprotein Ib-IX-V complex is stabilized by grp94/Hsp90b1 (show HSP90B1 ELISA Kits).
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 ELISA Kits) 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 ELISA Kits), GP1BB (show GP1BB ELISA Kits)) 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 ELISA Kits)) are defective in glycoprotein (GP)Ib-IX-V, a platelet-specific adhesion-signaling complex, composed of GPIbalpha (show GP1BA ELISA Kits) disulfide linked to GPIbbeta, and noncovalently associated with GPIX and GPV (show GP5 ELISA Kits).
GPIX increased the expression of GPIba (show GP1BA ELISA Kits) by promoting the formation of a disulfide bond between GPIba (show GP1BA ELISA Kits) and GPIbb (show GP1BB ELISA Kits) in transfected CHO (show COL11A1 ELISA Kits)-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/IIIa is the primary receptor set involved in platelet adhesion to adsorbed fibrinogen and serum albumin (show ALB ELISA Kits) 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 ELISA Kits) 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