Cytosol Nonspecific Dipeptidase 2, Recombinant, Human (CNDP2, CPGL, Glutamate Carboxypeptidase- Like Protein 1, Peptidase A, Tissue Carnosinase) Catalog number C9090-50 Supplier United States Biological The human CNDP2 gene encodes cytosol nonspecific dipeptidase, a member of the M20 family of metalloproteases (2, 3). Also known as glutamate carboxypeptidase-like protein 1 (CPGL), tissue carnosinase or peptidase A, CNDP2 is ubiquitously expressed throughout human tissues. Unlike CNDP1, CNDP2 has broad substrate specificity for dipeptides with free amino and carboxyl groups. Source Recombinant human cytosolic nonspecific dipeptidase encoded by the CNDP2 gene (human CNDP2, residue 1-475; Accession# Q96KP4) (1,2) was expressed with a C-terminal 10X His tag in Sf21 insect cells. Molecular Mass The purified rhCNDP2 migrates as three bands in SDS-PAGE with molecular masses of approximately 54, 38 and 22 kD. The 54 kD band corresponds to the full-length protein (485 amino acids). The 38 and 22 kD bands correspond to the N- and C-terminal fragments, respectively. The N-terminal sequencing of rhCNDP2 revealed only S 299HKKDILMHR, which corresponds to the N-terminus of the 22kD fragment. Endotoxin Level < 1.0 EU per 1 μg of the protein as determined by the LAL method. Activity Measure by its ability to cleave carnosine (β-Ala-His) in a two-step assay. See Activity Assay protocol on next page for details. The specific activity, as measured using the procedure above, is > 70 pmoles/min/μg. Storage Samples are stable for up to six months at -70° C in a manual defrost freezer after the receipt. After receiving, this enzyme can be aliquoted and stored under the above temperature for six months without a significant loss of activity. Avoid repeated freeze-thaw cycles. Formulation Supplied as a liquid in 25mM Tris, 0.15M NaCl, pH 7.5. Purity ≥ 95%, as determined by SDS-PAGE and visualized by silver stain. Grade Highly Purified Storage -70°C Antigen Modification Recombinant, Sf21 insect cells Reference 1. Strausberg, R.L. et al. 2002, Proc. Natl. Acad. Sci. USA 99:16899-16903. 2. Teufel, M. et al. 2003, J. Biol. Chem. 278:6521-6531. 3. Woessner, J. 2004, in Handbook of Proteolytic Enzymes (ed. Barrett, et al.) pp.1020-1022, Academic Press, San Diego. Powered by TCPDF (www.tcpdf.org).