Mouse Endoglin/CD105 Alexa Fluor® 647-conjugated Antibody Summary
Glu21-Gly581 (predicted)
Accession # NP_031958
Applications
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.
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Preparation and Storage
Background: Endoglin/CD105
Endoglin (CD105) is a 90 kDa type I transmembrane glycoprotein of the zona pellucida (ZP) family of proteins (1-3). Endoglin and betaglycan/T beta RIII are type III receptors for TGF beta superfamily ligands, sharing 71% amino acid (aa) identity within the transmembrane (TM) and cytoplasmic domains. Endoglin is highly expressed on proliferating vascular endothelial cells, chondrocytes, and syncytiotrophoblasts of term placenta, with lower amounts on hematopoietic, mesenchymal, and neural crest stem cells, activated monocytes, and lymphoid and myeloid leukemic cells (2-5). Mouse Endoglin cDNA encodes 653 aa including a 26 aa signal sequence, a 555 aa extracellular domain (ECD) with an orphan domain and a two-part ZP domain, a TM domain, and a 47 aa cytoplasmic domain (1-3). A mouse isoform with a 35 aa cytoplasmic domain (S-endoglin) can oppose effects of long (L) Endoglin (6, 7). The mouse Endoglin ECD shares 69%, 84%, 62%, 63%, and 66% aa identity with human, rat, bovine, porcine, and canine Endoglin, respectively. Endoglin homodimers interact with TGF-beta 1 and TGF-beta 3 (but not TGF-beta 2) but only after binding T beta RII (8). Similarly, they interact with activin-A and BMP-7 via activin type IIA or B receptors, and with BMP-2 via BMPR-1A/ALK-3 or BMPR-1B/ALK-6 (9). BMP-9, however, is reported to bind Endoglin directly (10). Endoglin modifies ligand-induced signaling in multiple ways. For example, expression of Endoglin can inhibit TGF-beta 1 signals but enhance BMP-7 signals in the same myoblast cell line (11). In endothelial cells, Endoglin inhibits T beta RI/ALK5 but enhances ALK1-mediated activation (12). Deletion of mouse Endoglin causes lethal vascular and cardiovascular defects, and human Endoglin haploinsufficiency can a cause the vascular disorder, hereditary hemorrhagic telangiectasia type I (13, 14). These abnormalities confirm the essential function of Endoglin in differentiation of smooth muscle, angiogenesis, and neovascularization (2-4, 12-14). In preeclampsia of pregnancy, high levels of proteolytically generated soluble Endoglin and VEGF R1 (sFlt-1), along with low placental growth factor (PlGF), are pathogenic due to anti-angiogenic activity (15).
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- Lebrin, F. and C.L. Mummery (2008) Trends Cardiovasc. Med. 18:25.
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Product Datasheets
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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