Human DPPIV/CD26 Alexa Fluor® 350-conjugated Antibody Summary
Accession # Q53TN1
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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
DPPIV/CD26 (EC 188.8.131.52) is a serine exopeptidase that releases Xaa-Pro dipeptides from the N-terminus of oligo- and polypeptides (1, 2). It is a type II membrane protein consisting of a short cytoplasmic tail, a transmembrane domain, and a long extracellular domain (3‑5). The extracellular domain contains glycosylation sites, a cysteine-rich region and the catalytic active site (Ser, Asp and His charge relay system). The amino acid sequence of the mouse DPPIV/CD26 extracellular domain is 84% and 91% identical to the human and rat counterparts, respectively. In the native state, DPPIV/CD26 is present as a noncovalently linked homodimer on the cell surface of a variety of cell types. The soluble form is also detectable in human serum and other body fluids, the levels of which may have clinical significance in patients with cancer, liver and kidney diseases, and depression. DPPIV/CD26 plays an important role in many biological and pathological processes. It functions as T cell-activating molecule (THAM). It serves as a cofactor for entry of HIV in CD4+ cells (6). It binds adenosine deaminase, the deficiency of which causes severe combined immunodeficiency disease in humans (7). It cleaves chemokines such as stromal-cell-derived factor 1 alpha and macrophage-derived chemokine (8, 9). It degrades peptide hormones such as glucagon (10). It truncates procalcitonin, a marker for systemic bacterial infections with elevated levels detected in patients with thermal injury, sepsis and severe infection, and in children with bacterial meningitis (11).
- Misumi and Ikehara (1998) in Handbook of Proteolytic Enzymes. Barrett, et al. (eds) San Diego: Academic Press, p. 378.
- Ikehara, et al. (1994) Methods Enzymol. 244:215.
- Marguet, et al. (1992) J. Biol. Chem. 267:2200.
- Bernard, et al. (1994) Biochemistry 33:15204.
- Viver, et al. (1991) J. Immunol. 147:447.
- Callebaut, et al. (1993) Science 262:2045.
- Kameoka, et al. (1993) Science 261:466.
- Ohtsuki, et al. (1998) FEBS Lett. 431:236.
- Proost, et al. (1999) J. Biol. Chem. 274:3988.
- Hinke, et al. (2000) J. Biol. Chem. 275:3827.
- Wrenger, et al. (2000) FEBS Lett. 466:155.
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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