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Human platelet glycoprotein V (GP5) is a part of the Ib-V-IX system of surface glycoproteins that constitute the receptor for von Willebrand factor (VWF; MIM 613160) and mediate the adhesion of platelets to injured vascular surfaces in the arterial circulation, a critical initiating event in hemostasis. Additionally we are shipping GP5 Antibodies (32) and and many more products for this protein.
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Desialylation of platelet VWFR therefore triggers platelet clearance and primes GPIbalpha (show GP1BA ELISA Kits) and GPV for MP-dependent cleavage.
GPV is cleaved upon agonist-induced platelet activation, with ADAM17 (show ADAM17 ELISA Kits) as the major enzyme mediating this process
GPIbalpha (show GP1BA ELISA Kits) and GPV are shed through an ADAM17 (show ADAM17 ELISA Kits)-dependent mechanism after aspirin administration
ROLE OF GPV IN HEMOSTASIS AND THROMBOSIS IS PROBABLY OF LESSER IMPORTANCE THAN PREVIOUSLY THOUGHT
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 (show GP9 ELISA Kits) and GPV.
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.
Both the high affinity thrombin receptor (show F2R ELISA Kits) (GPIb-IX-V) and GPIIb/IIIa are implicated in expression of thrombin (show F2 ELISA Kits)-induced platelet procoagulant activity.
laminin supports platelet adhesion depending on the interaction of VWF (show VWF ELISA Kits) and GPIb-IX-V under pathophysiological high shear flow
glycoprotein Ib-IX-V complex contributes to tissue factor (show F3 ELISA Kits)-independent thrombin (show F2 ELISA Kits) generation by recombinant factor VIIa on the activated platelet surface
Human platelet glycoprotein V (GP5) is a part of the Ib-V-IX system of surface glycoproteins that constitute the receptor for von Willebrand factor (VWF; MIM 613160) and mediate the adhesion of platelets to injured vascular surfaces in the arterial circulation, a critical initiating event in hemostasis. The main portion of the receptor is a heterodimer composed of 2 polypeptide chains, an alpha chain (GP1BA; MIM 606672) and a beta chain (GP1BB; MIM 138720), that are linked by disulfide bonds. The complete receptor complex includes noncovalent association of the alpha and beta subunits with platelet glycoprotein IX (GP9; MIM 173515) and GP5. Mutations in GP1BA, GP1BB, and GP9 have been shown to cause Bernard-Soulier syndrome (MIM 231200), a bleeding disorder (review by Lopez et al., 1998
glycoprotein 5 (platelet)
, platelet glycoprotein V
, glycoprotein V (platelet)
, platelet glycoprotein V-like
, Platelet glycoprotein 5
, Platelete glycoprotein 5
, glycoprotein 5, platelet
, glycoprotein 5