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GP6 encodes a platelet membrane glycoprotein of the immunoglobulin superfamily. Additionally we are shipping GP6 Antibodies (72) and GP6 Kits (27) and many more products for this protein.
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Inhibition of platelet activation by an anti-GPVI antibody significantly reduces infarct size.
These results demonstrate that GPVI is a receptor for fibrin and provide evidence that this interaction contributes to thrombus growth and stability.
data demonstrate that genetic deletion of GPVI receptor, FcRgamma (show FCER1G Proteins) chain, or the alpha2beta1 integrin changes the thrombotic potentials of these platelets to collagen dependent on the stimulus mechanism.
data suggest a novel role for FAK (show PTK2 Proteins) in GPVI-dependent ROS (show ROS1 Proteins) formation and platelet activation and elucidate a proximal signaling role for FAK (show PTK2 Proteins) within the GPVI pathway.
our results show that GPVI plays a dual role in inflammation by enhancing neutrophil-damaging activities while supporting the activation and hemostatic adhesion of single platelets to neutrophil-induced vascular breaches.
This study identifies GPVI as a platelet receptor for polymerized fibrin with 2 major functions: (1) amplification of thrombin (show F2 Proteins) generation and (2) recruitment of circulating platelets to clots.
Functional studies of platelets from Ceacam2 (show CEACAM2 Proteins)(-/-)-deficient mice (Cc2 (show TSG101 Proteins)(-/-)) revealed that CEACAM2 (show CEACAM2 Proteins) serves to negatively regulate collagen glycoprotein VI (platelet) (GPVI)-FcRgamma (show FCER1G Proteins)-chain and the C-type lectinlike receptor 2 (CLEC-2 (show CLEC1B Proteins)) signaling
Glaucocalyxin A inhibits platelet activation and thrombus formation preferentially via GPVI signaling pathway.
a delayed and markedly reduced thrombogenic response was still evident in VWF (show VWF Proteins)(-/-), GPVI, and alpha2beta1 blocked animals, suggesting that alternative primary hemostatic mechanisms can partially rescue the bleeding phenotype associated with these defects.
RhoG is expressed and activated in platelets, plays an important role in GPVI-Fc receptor gamma-chain (show FCER1G Proteins) complex-mediated platelet activation, and is critical for thrombus formation in vivo.
results support the idea that genetic variability of GP6 regulatory regions can be associated with platelet hyperaggregability - a possible cause of miscarriage
These results demonstrate that GP6 is a receptor for fibrin and provide evidence that this interaction contributes to thrombus growth and stability.
The plasma levels of sGPVI were the highest in patients with TMA without markedly reduced ADAMTS13 (show ADAMTS13 Proteins) and those were significantly reduced after plasma exchange.
Results suggest that variants of GP6 SNPs, namely, rs1671153, rs1654410, rs1654419, and rs1613662, may be associated with risk of recurrent miscarriage.
Lower platelet GPIV (show CD36 Proteins) levels are associated with no-reflow phenomenon in patients with acute myocardial infarction.
Studies indicate that Megakaryocyte maturation is accompanied by up-regulation of glycoprotein VI and down-regulation of leukocyte-associated immunoglobulin-like receptor-1 (show LAIR1 Proteins).
The identification of four unrelated homozygous patients with an identical defect suggests that inherited GPVI deficiency is more frequent than previously suspected, at least in Chile
This gene encodes a platelet membrane glycoprotein of the immunoglobulin superfamily. The encoded protein is a receptor for collagen and plays a critical role in collagen-induced platelet aggregation and thrombus formation. The encoded protein forms a complex with the Fc receptor gamma-chain that initiates the platelet activation signaling cascade upon collagen binding. Mutations in this gene are a cause of platelet-type bleeding disorder-11 (BDPLT11). Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
glycoprotein VI (platelet)
, glycoprotein 5
, platelet glycoprotein VI
, glycoprotein 6
, platelet collagen receptor