Detection of Human DPPIV/CD26 by Western Blot.
Western blot shows lysate of LoVo human colorectal adenocarcinoma cell line. PVDF membrane was probed with 2 µg/mL of Rat Anti-Human DPPIV/CD26 Monoclonal Antibody (Catalog # MAB1180) followed by HRP-conjugated Anti-Rat IgG Secondary Antibody (Catalog # HAF005). A specific band was detected for DPPIV/CD26 at approximately 110 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Preparation and Storage
Reconstitute at 0.5 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
DPPIV/CD26 (EC 220.127.116.11) 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.
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