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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 Kits (10) and Glycoprotein Ib (Platelet), alpha Polypeptide Proteins (9) and many more products for this protein.
Showing 10 out of 195 products:
Human Monoclonal GP1BA Primary Antibody for FACS - ABIN2663460
Clemetson, McGregor, James, Dechavanne, Lüscher et al.: Characterization of the platelet membrane glycoprotein abnormalities in Bernard-Soulier syndrome and comparison with normal by surface-labeling techniques and high-resolution two-dimensional gel ... in The Journal of clinical investigation 1982
Show all 6 references for ABIN2663460
Human Monoclonal GP1BA Primary Antibody for ICFC - ABIN2661721
Fox, Aggerbeck, Berndt: Structure of the glycoprotein Ib.IX complex from platelet membranes. in The Journal of biological chemistry 1988
Show all 6 references for ABIN2661721
Human Monoclonal GP1BA Primary Antibody for FACS, Func - ABIN125719
Bergmeier, Piffath, Goerge, Cifuni, Ruggeri, Ware, Wagner: The role of platelet adhesion receptor GPIbalpha far exceeds that of its main ligand, von Willebrand factor, in arterial thrombosis. in Proceedings of the National Academy of Sciences of the United States of America 2006
Show all 3 references for ABIN125719
Human Monoclonal GP1BA Primary Antibody for IHC (p) - ABIN180545
Hornby, Brown, Wilkinson, Mattock, Authi: Activation of human platelets by exposure to a monoclonal antibody, PM6/248, to glycoprotein IIb-IIIa. in British journal of haematology 1992
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Human Monoclonal GP1BA Primary Antibody for FACS, IF - ABIN1112144
Williams, Jackson: Analysis of populations of macrophage-granulocyte progenitor cells stimulated by activities in mouse lung-conditioned medium. in Experimental hematology 1978
Human Monoclonal GP1BA Primary Antibody for FACS - ABIN118647
Burgess, Lopez, Berndt, Dawes, Chesterman, Chong: Quinine-dependent antibodies bind a restricted set of epitopes on the glycoprotein Ib-IX complex: characterization of the epitopes. in Blood 1998
Dog (Canine) Polyclonal GP1BA Primary Antibody for WB - ABIN2784512
Maguire, Thakkinstian, Sturm, Levi, Lincz, Parsons, Whyte, Attia: Polymorphisms in platelet glycoprotein 1balpha and factor VII and risk of ischemic stroke: a meta-analysis. in Stroke; a journal of cerebral circulation 2008
both the gpIb-VWF (show VWF Antibodies) interaction and the integrin alpha(2 (show ITGA2 Antibodies))beta(1)-collagen interaction contribute to platelet adhesion under high shear stress; integrin alpha(II (show GSTA3 Antibodies))beta(1) makes a greater contribution to adhesion to type I collagen because less VWF (show VWF Antibodies) is bound
Thrombin (show F2 Antibodies) cleavage of platelet PAR4 (show F2RL3 Antibodies) 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 Antibodies)-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 Antibodies) interactions.
Platelet IKKbeta (show IKBKB Antibodies) 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 Antibodies) 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 (show GP5 Antibodies) 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 Antibodies) appears as a large, linear structure on the surface of 50% of the PT-VWD (show VWF Antibodies) 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 Antibodies) and factor XI and the resultant efficient activation of FXI (show F11 Antibodies)
Hemoglobin interaction with GP1balpha induces platelet activation and apoptosis: a novel mechanism associated with intravascular hemolysis.
Both GPIbalpha and PAR4 (show PAWR Antibodies) are required for thrombin (show F2 Antibodies)-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 Antibodies) stop codon in all 3 siblings
Whereas VWF (show VWF Antibodies)-D'D3 is the major regulator of soluble VWF (show VWF Antibodies) 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 Antibodies)) and glycoprotein Ibalpha (GPIbalpha).
data indicated that GPIIb (show ITGA2B Antibodies)-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 (show ITGA2B Antibodies)-IIIa and GPIb contents might be stimulated by elevated thrombopoietin (show THPO Antibodies)
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