CD26, Recombinant, Human, His-tag, Hi-5 (DPP IV, Dipeptidyl Peptidase IV, DPPIV, ADABP, ADCP2, TP103)

D26 is a complex enzyme expressed on the surface of most cell types and is a serine exopeptidase that cleaves x-proline dipeptides from the N-terminus of polypeptides. DPP4 protein is associated with intracellular signal transduction, apoptosis and plays an important role in tumor biology. There are at least 63 substrates which can bind specifically to DPP4 enzyme including growth factors, chemokines, neuro peptides. Furthermore, DPP4 plays a major role in glucose metabolism by cleaving incretins such as glucose-dependent insulinotropic polypeptide (GIP) and glucagon-like peptide-1 (GLP-1).\n\nRecombinant protein corresponding to aa39-766 of human CD26, with a C-terminal His-tag, expressed in high-5 cells using baculovirus expression system.\n\nTheoretical Molecular Weight: 86.4kD (746aa)\n(SDS-PAGE under denatured condition, apparent molecular weight of glycosylated rhDPP-4 protein will be appeared at approximately 90kD).\n\nBiological activity: \n(same/more than) 50units/mg\n\nUnit Definition: \nOne unit will hydrolyze 1umole of p-nitroaniline per minute at pH 8.0, at 37 degrees C using 1mM of Gly-Pro p-nitroanilde as a substrate.\n\nApplications: \nUseful for the study of enzyme kinetics, screening inhibitors and selectivity profiling. \n\nRecommended Dilution:\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

C2277-06J1

Size

100ug

Form

Supplied as a liquid in 20mM Tris-HCl, pH 8.0, 100mM sodium chloride, 1mM EDTA, 10% glycerol.

Purity

(same/more than) 95% by SDS PAGE

References

1. Pratley RE and Salsali A. (2007) Curr Med Res Opin. 23(4):919-31. 2. Rosenstock J. and Zinman B. (2007) Curr Opin Endocrino Diabetes Obes.60(11):1454-70. 3. Barnett A. (2006). J.Clin. Pract. 60(11):1454-70. 4. Davoodi, J., et al., (2007) Proteomics 7(13):2300-2310. 5. Hiramatsu, H., et al., (2007) Acta Biochim. Biophys. Sin. (Shanghai) 39(5):335-343.