Cytosol Nonspecific Dipeptidase 2, Recombinant, Human (CNDP2, CPGL, Glutamate Carboxypeptidase-Like Protein 1, Peptidase A, Tissue Carnosinase)

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.\n\nSource: \nRecombinant 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.\n\nMolecular Mass: \nThe 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.\n\nEndotoxin Level: \n< 1.0 EU per 1 microg of the protein as determined by the LAL method.\n\nActivity: \nMeasure by its ability to cleave carnosine (b-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/microg.\n\nStorage: \nSamples are stable for up to six months at -70 degrees 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.

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SPECIFICATIONS

Catalog Number

C9090-50

Size

10ug

Form

Supplied as a liquid in 25mM Tris, 0.15M NaCl, pH 7.5.

Purity

(same/more than) 95%, as determined by SDS-PAGE and visualized by silver stain.

References

1. Strausberg, R.L. et al. 2002, Proc. Natl. Acad. Sci. USA 99:16899-16903. \n2. Teufel, M. et al. 2003, J. Biol. Chem. 278:6521-6531. \n3. Woessner, J. 2004, in Handbook of Proteolytic Enzymes (ed. Barrett, et al.) pp.1020-1022, Academic Press, San Diego.