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Glycoprotein Ib (GP Ib) is a platelet surface membrane glycoprotein composed of a heterodimer, an alpha chain and a beta chain, that is linked by disulfide bonds. Zusätzlich bieten wir Ihnen Glycoprotein Ib (Platelet), alpha Polypeptide Antikörper (218) und Glycoprotein Ib (Platelet), alpha Polypeptide Kits (15) und viele weitere Produktgruppen zu diesem Protein an.
Showing 9 out of 15 products:
both the gpIb-VWF (zeige VWF Proteine) interaction and the integrin alpha(2 (zeige ITGA2 Proteine))beta(1)-collagen interaction contribute to platelet adhesion under high shear stress; integrin alpha(II (zeige GSTA3 Proteine))beta(1) makes a greater contribution to adhesion to type I collagen because less VWF (zeige VWF Proteine) is bound
this study shows that atheroma formation is inhibited in GPIba-deficient mice on atherosclerosis-prone background
allosteric inhibitor SbO4L targets the glycoprotein Ibalpha-binding and heparin-binding site of thrombin (zeige F2 Proteine)
Thrombin (zeige F2 Proteine) cleavage of platelet PAR4 (zeige F2RL3 Proteine) promotes leukocyte recruitment to sites of vascular injury. This process is negatively regulated by GPIbalpha.
GPIbalpha-mediated interactions between platelets and endothelial cells, as well as leukocytes, support innate immune cell recruitment and promote arteriogenesis-establishing platelets as critical players in this process.
Atherosclerosis reduction in mice lacking GPIbalpha may not result from the defective GPIbalpha-ligand binding, but more likely is a consequence of functional defects of GPIbalpha-/- platelets and reduced blood platelet counts.
Data suggest that targeting platelet receptor glycoprotein Ibalpha (GPIbalpha)-von Willebrand factor VWF (zeige VWF Proteine)-A1 binding interface may offer a therapeutic approach to reducing platelet-driven thrombosis.
Following endothelial damage, platelet cross-linking during closure of the vessel lumen is mediated by GPIbalpha-VWF (zeige VWF Proteine) interactions.
Platelet IKKbeta (zeige IKBKB Proteine) deficiency increases the formation of injury-induced arterial neointimal tissue via delayed glycoprotein Ibalpha shedding.
these data demonstrate that coordinated expression of GPIbalpha and filamin (zeige FLNA Proteine) is required for efficient trafficking of either protein to the cell surface, and for production of normal-sized platelets.
Desialylation of platelet VWFR therefore triggers platelet clearance and primes GPIbalpha and GPV for MP-dependent cleavage.
The >30 nm macroglycopeptide separating the two domains of GPIbalpha transmits force on the VWF (zeige VWF Proteine)-GPIbalpha bond (whose lifetime is prolonged by leucine-rich repeat domain unfolding) to the juxtamembrane mechanosensitive domain to enhance its unfolding, resulting in unfolding cooperativity at an optimal force.
Meta-analysis found that glycoprotein Ia (zeige MMRN1 Proteine) C807T T allele or the TT genotype, the Ser (zeige SIGLEC1 Proteine)-allele of HPA-3 and B allele of glycoprotein Ibalpha variable number tandem repeat polymorphisms were associated with increased risk for ischemic stroke.
Our results suggest that the -5CC genotype in Kozak sequence of GPIb-alpha may be associated with a higher risk of developing arterial ischemia of lower limbs in type 2 diabetes mellitus patients.
Specific inhibition of GPIbalpha shedding in the stored platelets improves post-transfusion platelet recovery and hemostatic function, providing clear evidence for GPIbalpha shedding as a cause of platelet clearance.
miR (zeige MLXIP Proteine)-10a and miR10b regulate the expression of human platelet GP1BA and GP1bb (zeige GP1BB Proteine) for normal megakaryopoiesis.
Data indicate that binding of hemoblobin (Hb) to glycoprotein1balpha (GP1balpha) induced platelet activation plays a crucial role in thrombus formation on immobilized von Willebrand factor (VWF (zeige VWF Proteine)) or type I collagen under shear stresses.
Lateral dimerization of GPIbalpha induced by antibody binding is not sufficient to initiate GPIb-IX signaling and induce platelet clearance.
GPIb alpha plays a critical role in the co-localization of thrombin (zeige F2 Proteine) and factor XI and the resultant efficient activation of FXI (zeige F11 Proteine)
Hemoglobin interaction with GP1balpha induces platelet activation and apoptosis: a novel mechanism associated with intravascular hemolysis.
Glycoprotein Ib (GP Ib) is a platelet surface membrane glycoprotein composed of a heterodimer, an alpha chain and a beta chain, that is linked by disulfide bonds. The Gp Ib functions as a receptor for von Willebrand factor (VWF). The complete receptor complex includes noncovalent association of the alpha and beta subunits with platelet glycoprotein IX and platelet glycoprotein V. The binding of the GP Ib-IX-V complex to VWF facilitates initial platelet adhesion to vascular subendothelium after vascular injury, and also initiates signaling events within the platelet that lead to enhanced platelet activation, thrombosis, and hemostasis. This gene encodes the alpha subunit. Several polymorphisms and mutations have been described in this gene, some of which are the cause of Bernard-Soulier syndromes and platelet-type von Willebrand disease.
glycoprotein 1b, alpha polypeptide
, platelet glycoprotein Ib alpha chain
, glycoprotein Ib (platelet), alpha polypeptide
, platelet glycoprotein Ib alpha polypeptide
, GP-Ib alpha
, glycoprotein Ibalpha
, antigen CD42b-alpha
, platelet membrane glycoprotein 1b-alpha subunit