protein

Platelet Glycoprotein Ib alpha, Recombinant, Human (PGIb alpha)

MBS636761

0.05 mg

740 USD

Recombinant Protein

Platelet Glycoprotein Ib alpha, Recombinant, Human (PGIb alpha)

[Platelet Glycoprotein Ib alpha]

[platelet glycoprotein Ib alpha chain; Platelet glycoprotein Ib alpha chain; platelet glycoprotein Ib alpha chain; GP-Ib alpha; antigen CD42b-alpha; platelet membrane glycoprotein 1b-alpha subunit; glycoprotein Ib (platelet), alpha polypeptide; Antigen CD42b-alpha]

[GP1BA; GP1BA; BSS; GP1B; VWDP; CD42B; GPIbA; BDPLT1; BDPLT3; DBPLT3; CD42b-alpha; GP-Ib alpha; GPIb-alpha; GPIbA]

GP1BA_HUMAN

Mouse

>90% as determined by SDS-PAGE under reducing conditions and visualized by silver strain.

Supplied as a lyophilized powder in PBS. Reconstitute with PBS to 100ug/ml.

Lyophilized powder may be stored at -20°C. Stable for 12 months at -20°C. Reconstitute with sterile PBS. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Reconstituted product is stable for 6 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

N-Terminal Sequence Analysis: His 17. SDS-PAGE: ~95-120kD,reducing conditions. Endotoxin Level: <0.10 EU per 1 ug of the protein by the LAL method. Activity: Measured by its binding ability in a functional ELISA. Recombinant Human CD42b/GPIB alpha is inmobilized at 0.5 ug/mL(100uL/well),the concentration of Recombinant Human vWF-A2 that produces 50% optimal binding respones is~6-36 ng/mL in the presence of ristocerin.

Source Note: Mouse myeloma cell line, NS0-derived human CD42b/GPIb alpha protein His17-Leu505, with a C-terminal 6-His tag. Immunogen: A DNA sequence encoding the extracellular domain of human GPIb A (His 17-Lys 505; Accession # P07359) was fused with a six-histidine tag at the C-terminus. The protein was expressed in NS0 cells line.

Molecular Biology; MB-Carbohydrates, Glycoproteins

Platelet glycoprotein Ib alpha chain (GPIb a), also known as CD42ba, is a 145kD type I transmembrane protein that is a member of the leucine-rich repeat (LRR) family of ligand binding proteins.1-3 It is expressed by platelets as the ligand-binding subunit of the platelet GPIb-IX-V complex.4 Human GPIb a contains a 16 amino acid (aa) signal sequence, a 489 aa extracellular domain (ECD), a 21-aa transmembrane domain, and a 100 aa cytoplasmic region. The ECD contains 8 LRRs, with # 2, 3 and 4 having been demonstrated to regulate shear-dependent adhesion to von Willebrand factor (vWF).5, 6 The LRRs are followed by a thrombin-binding anionic region that includes three sulfated tyrosines, a sialomucin domain with N- and O-linked carbohydrates, and two cysteines near the membrane that allow dimerization with GP1bb.1-6 Four human isoforms with 1 to 4 repeats of aa 398-411 within the sialomucin domain of mature GPIb a are known to exist but have unknown significance.7 The ECD of human GPIb a shares 48-51% aa identity with mouse, rat, bovine and canine GPIb a. The metalloproteinase TACE/ADAM17 constitutively and inducibly cleaves GPIb a, between Gly 480 and Val 481. This releases a soluble form called glycocalicin that circulates at ~2 ug/mL.8, 9 GPIb a binding to ligands such as thrombin, kininogen, and coagulation factors XI and XII helps to initiate platelet activation and coordinate the coagulation cascade.1, 10-12 Binding of GPIb a to vWF or thrombospondin in the plasma or matrix, vWF or P-selectin on endothelial cells, or the integrin aMb2 (MAC-1) on myeloid cells, controls response to vascular injury. A DNA sequence encoding the extracellular domain of human GPIb A (His 17-Lys 505; Accession # P07359) was fused with a six-histidine tag at the C-terminus. The protein was expressed in NS0 cells line. Calculated molecular mass of ~ 54.7kD. As a result of glycosylation, recombinant human GPIb a migrates as an ~ 95-120kD protein in SDS-PAGE under reducing conditions.

291190772

NP_000164.5

NM_000173.5

P07359

54.7 kDa

ECM-receptor Interaction Pathway (83068); ECM-receptor Interaction Pathway (479); Formation Of Fibrin Clot (Clotting Cascade) Pathway (106057); GP1b-IX-V Activation Signalling Pathway (187205); Hematopoietic Cell Lineage Pathway (83078); Hematopoietic Cell Lineage Pathway (489); Hemostasis Pathway (106028); Intrinsic Pathway (106059); Platelet Adhesion To Exposed Collagen Pathway (106030); Platelet Aggregation (Plug Formation) Pathway (106053)

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. [provided by RefSeq, Mar 2010]

GPIbA: GP-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to the A1 domain of vWF, which is already bound to the subendothelium. Genetic variations in GP1BA may be a cause of susceptibility to non-arteritic anterior ischemic optic neuropathy (NAION). NAION is an ocular disease due to ischemic injury to the optic nerve. It usually affects the optic disk and leads to visual loss and optic disk swelling of a pallid nature. Visual loss is usually sudden, or over a few days at most and is usually permanent, with some recovery possibly occurring within the first weeks or months. Patients with small disks having smaller or non-existent cups have an anatomical predisposition for non-arteritic anterior ischemic optic neuropathy. As an ischemic episode evolves, the swelling compromises circulation, with a spiral of ischemia resulting in further neuronal damage. Defects in GP1BA are a cause of Bernard-Soulier syndrome (BSS); also known as giant platelet disease (GPD). BSS patients have unusually large platelets and have a clinical bleeding tendency. Defects in GP1BA are the cause of benign mediterranean macrothrombocytopenia (BMM); also known as autosomal dominant benign Bernard-Soulier syndrome. BMM is characterized by mild or no clinical symptoms, normal platelet function, and normal megakaryocyte count. Defects in GP1BA are the cause of pseudo-von Willebrand disease (VWDP). A bleeding disorder is caused by an increased affinity of GP-Ib for soluble vWF resulting in impaired hemostatic function due to the removal of vWF from the circulation. Protein type: Membrane protein, integral; Cell surface; Cell adhesion. Chromosomal Location of Human Ortholog: 17p13.2. Cellular Component: anchored to external side of plasma membrane; cell surface; membrane; integral to plasma membrane; plasma membrane. Molecular Function: protein binding; thrombin receptor activity. Biological Process: platelet activation; fibrinolysis; cell surface receptor linked signal transduction; regulation of blood coagulation; cell morphogenesis; blood coagulation; cell adhesion; blood coagulation, intrinsic pathway. Disease: Pseudo-von Willebrand Disease; Bernard-soulier Syndrome; Bernard-soulier Syndrome, Type A2, Autosomal Dominant; Nonarteritic Anterior Ischemic Optic Neuropathy, Susceptibility To

0.05 mg

740 USD