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  Dipeptidyl Peptidase IV (CD26), Porcine Kidney
Cat. No. 317640  
All Categories » Calbiochem » Proteins and Enzymes » Proteases » Peptidases and Related

CD26
DPPIV

Liquid. In 20 mM Tris-HCl, 5 mM CaCl2, 1 µM ZnCl2, 0.05% NaN3, pH 8.0. AVOID FREEZE/THAW CYCLES. Native, DPP IV purified from porcine kidney (renal brush border of the proximal tubule). A serine exopeptidase dimer composed of two identical subunits of 110-130 kDa. Cleaves Xaa-Pro dipeptides from the N-terminus of oligo and polypeptides. DPPIV is involved in many cellular processes such as activation of cytokines, differentiation, T cell activation, and cell-matrix interactions. Inhibition of DPPIV has been reported to be an effective treatment for type II diabetes. MW: ~210000-260000 (unreduced). Specific activity: ≥35 units/mg protein. One unit is defined as the amount of enzyme that will hydrolyze 1.0 µmole 7-(Gly-Pro)-amino-4-methylcoumarinamide per min at 37°C, pH 8.5. Purity: ≥90% by SDS-PAGE. EC 3.4.14.5.

Ref.: Bar, J., et al. 2003. Biol. Chem. 384, 1553. Engel, M., et al. 2003. Proc. Natl. Acad. Sci. USA 100, 5063. Ikehara, Y., et al. 1994. Methods. Enzymol. 244, 215. David, F., et al. 1993. J. Biol. Chem. 268, 17247. Thomsen, P.D., et al. 1993. Mamm. Genome 4, 604. Misumi, Y., et al. 1992. Biochim. Biophys. Acta. 1131, 333. Seidl, R., et al. 1991. Biol. Chem. Hoppe Seyler 372, 213. Checler, F., et al. 1985. J. Neurochem. 45, 1509. Imai, K., et al. 1983. J. Biochem. 93, 431. Kato, T., et al. 1979. Experientia. 35, 409. Kojima, K., et al. 1979. Anal. Biochem. 100, 43. Kato, T., et al. 1978. Biochem. Med. 19, 351. Kenny, A.J., et al. 1976. Biochem. J. 157, 169.

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All Categories » Calbiochem » Proteins and Enzymes » Proteases » Peptidases and Related