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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 (216) and Glycoprotein Ib (Platelet), alpha Polypeptide Kits (20) and many more products for this protein.
Showing 9 out of 15 products:
Combined deficiency of factors V and VIII (show COX8A Proteins) by chance coinheritance of parahaemophilia and haemophilia A, but not by mutations of either LMAN1 (show LMAN1 Proteins) or MCFD2 (show MCFD2 Proteins)
ERK5 (show MAPK7 Proteins) associates with CKII (show CSNK2A1 Proteins) to play essential roles in GPIb-IX-mediated platelet activation via the PTEN/PI3K (show PIK3CA Proteins)/Akt (show AKT1 Proteins) pathway.
There was no evidence to suggest that polymorphisms of GP VI T13254C and GP Ibalpha VNTR were associated with CAD.
analysis of an artificial botrocetin that can inhibit the VWF (show VWF Proteins)-GPIb interaction
Loss of the platelet surface receptors GPIbalpha and GPVI (show GP6 Proteins) in heart failure, CF-VAD (show KCTD1 Proteins) and ECMO patients may contribute to ablated platelet adhesion/activation, and limit thrombus formation under high/pathologic shear conditions
Very low birth weight preterm neonates have increased numbers of platelets interacting with von Willebrand Factor (show VWF Proteins), and increased GPIbalpha expression on the platelet surface
Data suggest that an aspartate at position 1261 is the most critical residue of VWF (show VWF Proteins) N-terminal linker for inhibiting binding of VWF (show VWF Proteins) A1 domain to GP1BA on platelets in a model simulating blood flow velocity; network of salt bridges between Asp1261 and rest of VWF (show VWF Proteins) A1 domain lock N-terminal linker in place such that binding to GP1BA is reduced.
Data show that von Willebrand factor (VWF (show VWF Proteins)) is first converted from a compact to linear form by flow, and is subsequently activated to bind platelet glycoprotein Ib alpha polypeptide (show ITGAE Proteins) (GPIbalpha) in a tension-dependent manner.
The >30 nm macroglycopeptide separating the two domains of GPIbalpha transmits force on the VWF (show VWF Proteins)-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 (show MMRN1 Proteins) C807T T allele or the TT genotype, the Ser (show SIGLEC1 Proteins)-allele of HPA-3 and B allele of glycoprotein Ibalpha variable number tandem repeat polymorphisms were associated with increased risk for ischemic stroke.
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
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 (show F2 Proteins)
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.
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.
, antigen CD42b-alpha
, platelet glycoprotein Ib alpha chain
, platelet membrane glycoprotein 1b-alpha subunit
, glycoprotein Ib (platelet), alpha polypeptide
, platelet glycoprotein Ib alpha polypeptide
, glycoprotein Ibalpha
, glycoprotein 1b, alpha polypeptide
, platelet glycoprotein Ib alpha chain-like