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Platelet glycoprotein Ib (GPIb) is a heterodimeric transmembrane protein consisting of a disulfide-linked 140 kD alpha chain and 22 kD beta chain. Additionally we are shipping GP1BB Antibodies (30) and GP1BB Kits (9) and many more products for this protein.
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Rare variants in GP1BB are responsible for autosomal dominant macrothrombocytopenia.
miR (show MLXIP Proteins)-10a and miR10b regulate the expression of human platelet GP1BA (show GP1BA Proteins) and GP1bb for normal megakaryopoiesis.
Data show that localization of the GP Ib-IX complex to the lipid domain is mediated by GP Ibbeta and GP IX (show GP9 Proteins) transmembrane domains.
Low levels of CD9 (show CD9 Proteins) coincidental with a novel nonsense mutation in glycoprotein Ibbeta in a patient with Bernard-Soulier syndrome.
genetic association study in population in western India: Data suggest novel mutations in platelet glycoprotein Ib (GP1BA (show GP1BA Proteins), GP1BB) and GP9 (show GP9 Proteins) are associated with Bernard-Soulier syndrome in subjects studies; of 12 mutations identified, ten were novel.
a suspicion of 22q11.2 deletion is warranted in pediatric BSS (show GP1BA Proteins) patients with a mutation in the GPIbbeta gene, even without remarkable symptoms.
Studies indicate that platelets from Bernard-Soulier syndrome (BSS) are defective in glycoprotein (GP)Ib-IX-V, a platelet-specific adhesion-signaling complex, composed of GPIbalpha disulfide linked to GPIbbeta, and noncovalently associated with GPIX and GPV.
GPIbbeta missense mutations from Bernard-Soulier syndrome were examined for changes to GPIb-IX complex surface expression. Mutations A108P and P74R were found to maintain normal secretion/folding of GPIbbeta(E) but were unable to support GPIX (show GP9 Proteins) surface expression
GPIIb/IIIa is the primary receptor set involved in platelet adhesion to adsorbed fibrinogen and serum albumin (show ALB Proteins) irrespective of their degree of adsorption-induced unfolding, while the GPIb-IX-V receptor complex plays an insignificant role.
GP Ibbeta/GP IX (show GP9 Proteins) mediates the disulfide-linked GP Ibalpha localization to the GEMs, which is critical for vWf (show VWF Proteins) interaction at high shear
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.
Role of GPIbbeta in modulating vWF (show VWF Proteins) mediated platelet adhesion.
Platelet glycoprotein Ib (GPIb) is a heterodimeric transmembrane protein consisting of a disulfide-linked 140 kD alpha chain and 22 kD beta chain. It is part of the GPIb-V-IX system that constitutes the receptor for von Willebrand factor (VWF), and mediates platelet adhesion in the arterial circulation. GPIb alpha chain provides the VWF binding site, and GPIb beta contributes to surface expression of the receptor and participates in transmembrane signaling through phosphorylation of its intracellular domain. Mutations in the GPIb beta subunit have been associated with Bernard-Soulier syndrome, velocardiofacial syndrome and giant platelet disorder. The 206 amino acid precursor of GPIb beta is synthesized from a 1.0 kb mRNA expressed in plateletes and megakaryocytes. A 411 amino acid protein arising from a longer, unspliced transcript in endothelial cells has been described\; however, the authenticity of this product has been questioned. Yet another less abundant GPIb beta mRNA species of 3.5 kb, expressed in nonhematopoietic tissues such as endothelium, brain and heart, was shown to result from inefficient usage of a non-consensus polyA signal in the neighboring upstream gene (SEPT5, septin 5). In the absence of polyadenylation from its own imperfect site, the SEPT5 gene produces read-through transcripts that use the consensus polyA signal of this gene.
glycoprotein Ib (platelet), beta polypeptide
, GP-Ib beta
, antigen CD42b-beta
, nuclear localization signal deleted in velocardiofacial syndrome
, platelet glycoprotein Ib beta chain
, glycoprotein Ib, beta polypeptide