Human Syndecan-2/CD362 Alexa Fluor® 405-conjugated Antibody Summary
Accession # AAH49836
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Syndecan-2, previously known as fibroglycan or heparan sulfate proteoglycan, is a member of the syndecan family of Type 1 transmembrane proteins capable of carrying heparan sulfate (HS) and chondroitin sulfate glycosaminoglycans. The four vertebrate syndecans show conserved cytoplasmic domains and divergent extracellular portions (except for GAG attachment sites). Among the Syndecans, Syndecan-2 is most similar to Syndecan-4 (1‑3). Human Syndecan-2 is synthesized as a 201 amino acid (aa) core protein with an 18 aa signal sequence, a 126 aa extracellular domain (ECD), a 25 aa transmembrane region and a 32 aa cytoplasmic tail (4). The human ECD of Syndecan-2 contains three closely-spaced consensus Ser-Gly sequences for the attachment of HS side chains. It shares 76%, 73%, 87%, 78% and 63% aa identity with the ECD of mouse, rat, bovine, canine and chicken Syndecan-2, respectively. The cytoplasmic tail has both serine and tyrosine phosphorylation sites. Addition of 20‑80 disaccharides per side chain adds considerably to the size of the 22 kDa core protein. Non-covalent homodimerization of Syndecan-2 is dependent on the transmembrane domain (5). Syndecan-2 is expressed in cells of mesenchymal origin, neuronal and epithelial cells, and is the predominant syndecan expressed during embryonic development. Expression is upregulated in several cancer cell lines (6). After induction in macrophages by inflammatory mediators, Syndecan-2 selectively binds FGFbasic, VEGF and EGF (7). Syndecan-2 expressed on human primary osteoblasts binds GM-CSF and may function as a co‑receptor (8). Activated endothelial cell Syndecan-2 specifically binds IL-8 and may participate in promoting neutrophil extravasation by forming a chemotactic IL-8 gradient (9). Typically, cytokine, chemokine and extracellular matrix protein binding occurs through interaction with HS side chains, but the Syndecan-2 extracellular domain can bind TGF-beta directly via protein-protein interaction (10).
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- Oh, E.-S, and J. R. Couchman (2004) Mol. Cells 17:181.
- Essner, J. J. et al. (2006) Int. J. Biochem. Cell Biol. 38:152.
- Marynen, P. et al. (1989) J. Biol. Chem. 264:7017.
- Choi, S. et al. (2005) J. Biol. Chem. 280:42573.
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- Clasper, S. et al. (1999) J. Biol. Chem. 274:24113.
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- Halden, Y. et al. (2004) Biochem. J. 377:533.
- Chen, L. et al. (2004) J. Biol. Chem. 279:15715.
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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