Human PEAR1 Alexa Fluor® 750-conjugated Antibody Summary
Accession # Q5VY43
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
Platelet endothelial aggregation receptor 1 (PEAR1) is a 150 kDa type I transmembrane protein and member of the MEGF family of proteins (1). Human PEAR1 is synthesized as a 1037 amino acid (aa) precursor that contains a 20 aa signal sequence, a 735 aa extracellular domain (ECD), a 21 aa transmembrane region, and a 261 aa cytoplasmic region. The ECD consists of 15 EGF-like repeats that vary in length from 39 to 42 aa and contain a consensus sequence of CX1-2GX2GX2-4CX3CX1-3CX1-2GX1-2CX4GX1CX1CX2GX2GX2C (1). The consensus repeat contains six conserved glycine residues and eight conserved cysteine residues, suggesting four disulfide-bonded cysteine pairs in each EGF repeat (1). Within the ECD, there are also five potential sites for N-linked glycosylation. The cytoplasmic region contains five potential Src homology 3-binding, proline-rich domains (1). Mature human PEAR1 is 84% aa identical to mature mouse PEAR1. PEAR1 is most highly expressed in platelets and endothelial cells (1). Functionally, PEAR1 is a receptor for a yet undetermined ligand that signals upon the formation of platelet‑platelet contacts induced both by platelet aggregations and by platelet centrifugation (1). The signaling enhances and stabilizes platelet thrombi (2). Upon aggregation, the surface-expressed protein is tyrosine-phosphorylated (1). This phosphorylation event is inhibited by the alpha IIb beta 3 antagonist eptifibatide, thus demonstrating that PEAR1 tyrosine phosphorylation is dependent on surface contacts between activated platelets (1). PEAR1 can be phosphorylated in an alpha IIb beta 3 integrin-dependent manner on tyrosine (Tyr925) and serine residues (Ser593 and Ser1029) and, potentially, at Tyr804, Tyr943, and Tyr979 (1). Inherited PEAR1 variations that alter expression or function of the platelet signaling molecule could modify agonist-induced aggregation in native platelets (2). In addition, a genetic variant in PEAR1 could be an important determinant of residual platelet function during aspirin treatment, because the COX1/thromboxane A2 pathway will be strongly inhibited by aspirin, and maximal aggregation will then be dependent on other secondary signaling pathways (2).
- Nanda, N. et al. (2005) J. Biol. Chem. 280:24680.
- Herrera-Galeano, J.E. et al. (2008) Arterioscler. Thromb. Vasc. Biol. 28:1484.
Product Specific Notices
This product is provided under an agreement between Life Technologies Corporation and R&D Systems, Inc, and the manufacture, use, sale or import of this product is subject to one or more US patents and corresponding non-US equivalents, owned by Life Technologies Corporation and its affiliates. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The sale of this product is expressly conditioned on the buyer not using the product or its components (1) in manufacturing; (2) to provide a service, information, or data to an unaffiliated third party for payment; (3) for therapeutic, diagnostic or prophylactic purposes; (4) to resell, sell, or otherwise transfer this product or its components to any third party, or for any other commercial purpose. Life Technologies Corporation will not assert a claim against the buyer of the infringement of the above patents based on the manufacture, use or sale of a commercial product developed in research by the buyer in which this product or its components was employed, provided that neither this product nor any of its components was used in the manufacture of such product. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, Cell Analysis Business Unit, Business Development, 29851 Willow Creek Road, Eugene, OR 97402, Tel: (541) 465-8300. Fax: (541) 335-0354.
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