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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. Additionally we are shipping Glycoprotein Ib (Platelet), alpha Polypeptide Antibodies (195) and Glycoprotein Ib (Platelet), alpha Polypeptide Kits (10) and many more products for this protein.
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both the gpIb-VWF (show VWF Proteins) interaction and the integrin alpha(2 (show ITGA2 Proteins))beta(1)-collagen interaction contribute to platelet adhesion under high shear stress; integrin alpha(II (show GSTA3 Proteins))beta(1) makes a greater contribution to adhesion to type I collagen because less VWF (show VWF Proteins) is bound
Thrombin (show F2 Proteins) cleavage of platelet PAR4 (show F2RL3 Proteins) 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 (show VWF Proteins)-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 (show VWF Proteins) interactions.
Platelet IKKbeta (show IKBKB Proteins) 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 (show FLNA Proteins) 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.
miscarriage occurred in the majority of pregnancies in a model of anti-GPIbalpha-mediated fetal and neonatal immune thrombocytopenia (FNIT), which was far more frequent than in anti-integrinbeta3-mediated FNIT
Data show that the surface-bound VWF (show VWF Proteins) appears as a large, linear structure on the surface of 50% of the PT-VWD (show VWF Proteins) platelets.
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 (show F2 Proteins) and factor XI and the resultant efficient activation of FXI (show F11 Proteins)
Hemoglobin interaction with GP1balpha induces platelet activation and apoptosis: a novel mechanism associated with intravascular hemolysis.
Both GPIbalpha and PAR4 (show PAWR Proteins) are required for thrombin (show F2 Proteins)-induced reactive oxygen species formation
Report no relationship, between polymorphisms of platelet membrane glycoprotein Ibalpha and risk of coronary heart disease in Chinese Han population.
Molecular analysis demonstrated a novel homozygous c.800C>G substitution in GP1BA exon 2 leading to a serine 267 Ter (show TECR Proteins) stop codon in all 3 siblings
Whereas VWF (show VWF Proteins)-D'D3 is the major regulator of soluble VWF (show VWF Proteins) binding to platelet GpIbalpha, both the D'D3-domain and N-terminal peptide regulate platelet translocation and thrombus formation.
Data indicate that GPIbalpha clustering induced by anti-GPIbalpha N-terminus antibody causes integrin alphaIIbbeta3-dependent platelet aggregation, phagocytosis, and rapid platelet clearance in the liver.
Data show that force can switch the kinetics of bond formation between A1 domain of von Willebrand factor (VWF (show VWF Proteins)) and glycoprotein Ibalpha (GPIbalpha).
data indicated that GPIIb-IIIa and GPIb levels are mainly affected by platelet size (MPV) but not by their genetic variations; in some acute coronary syndrome patients, production of large platelets with high GPIIb-IIIa and GPIb contents might be stimulated by elevated thrombopoietin (show THPO Proteins)
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