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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 Kits (25) and and many more products for this protein.
Showing 10 out of 29 products:
Mouse (Murine) Monoclonal GP5 Primary Antibody for FACS - ABIN2662644
Andrews, Harris, McNally, Berndt: Binding of purified 14-3-3 zeta signaling protein to discrete amino acid sequences within the cytoplasmic domain of the platelet membrane glycoprotein Ib-IX-V complex. in Biochemistry 1998
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Mouse (Murine) Monoclonal GP5 Primary Antibody for FACS - ABIN2664689
Hickey, Hagen, Yagi, Roth: Human platelet glycoprotein V: characterization of the polypeptide and the related Ib-V-IX receptor system of adhesive, leucine-rich glycoproteins. in Proceedings of the National Academy of Sciences of the United States of America 1993
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Mouse (Murine) Monoclonal GP5 Primary Antibody for FACS - ABIN2660118
Inoue, Suzuki-Inoue, Ozaki: Redundant mechanism of platelet adhesion to laminin and collagen under flow: involvement of von Willebrand factor and glycoprotein Ib-IX-V. in The Journal of biological chemistry 2008
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Mouse (Murine) Monoclonal GP5 Primary Antibody for ICFC - ABIN2658230
Ravanat, Morales, Azorsa, Moog, Schuhler, Grunert, Loew, Van Dorsselaer, Cazenave, Lanza: Gene cloning of rat and mouse platelet glycoprotein V: identification of megakaryocyte-specific promoters and demonstration of functional thrombin cleavage. in Blood 1997
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Mouse (Murine) Monoclonal GP5 Primary Antibody for IHC (fro), FACS - ABIN2689254
Sato, Kiyokawa, Taguchi, Suzuki, Sekino, Ohmi, Itagaki, Sato, Lepage, Lanza, Fujimoto: Functional conservation of platelet glycoprotein V promoter between mouse and human megakaryocytes. in Experimental hematology 2000
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Human Monoclonal GP5 Primary Antibody for Func, IF - ABIN1106368
Modderman, Admiraal, Sonnenberg, von dem Borne: Glycoproteins V and Ib-IX form a noncovalent complex in the platelet membrane. in The Journal of biological chemistry 1992
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Desialylation of platelet VWFR therefore triggers platelet clearance and primes GPIbalpha (show GP1BA Antibodies) and GPV for MP-dependent cleavage.
GPV is cleaved upon agonist-induced platelet activation, with ADAM17 (show ADAM17 Antibodies) as the major enzyme mediating this process
GPIbalpha (show GP1BA Antibodies) and GPV are shed through an ADAM17 (show ADAM17 Antibodies)-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 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 (show GP9 Antibodies) and GPV.
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.
Both the high affinity thrombin receptor (show F2R Antibodies) (GPIb-IX-V) and GPIIb (show ITGA2B Antibodies)/IIIa are implicated in expression of thrombin (show F2 Antibodies)-induced platelet procoagulant activity.
laminin supports platelet adhesion depending on the interaction of VWF (show VWF Antibodies) and GPIb-IX-V under pathophysiological high shear flow
glycoprotein Ib-IX-V complex contributes to tissue factor (show F3 Antibodies)-independent thrombin (show F2 Antibodies) 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