101 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
92 kDa, reducing conditions
Publications
Read Publications using 5419-SE in the following applications:
Store the unopened product at -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date.
Buffer
Supplied as a 0.2 μm filtered solution in Tris, NaCl and Glycerol.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human DPP9 Protein, CF
dipeptidyl peptidase 9
Dipeptidyl peptidase IV-related protein 2
dipeptidyl peptidase IV-related protein-2
Dipeptidyl peptidase IX
Dipeptidyl peptidase-like protein 9
dipeptidylpeptidase 9
dipeptidyl-peptidase 9
DKFZp762F117
DP9
DPLP9
DPP IX
DPP9
DPRP2
DPRP-2
EC 3.4.14.5
FLJ16073
Background
DPP9 is a member of the S9b family of serine peptidases (1, 2). It shares 19% amino acid identity with DPP4 and 58% amino acid identity with DPP8. It exhibits post‑proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-terminus of oligo- and polypeptides (3). Unlike DPP4, DPP9 does not appear to be membrane bound and is localized exclusively in the cytoplasm (4). This family of proline-specific dipeptidyl peptidases has been implicated in a variety of diseases including type 2 diabetes, obesity and cancer, and has been a potential target for drug discovery (5, 6).
Olsen, C. and Wagtmann, N. (2002) Gene 299:185.
Qi, S.Y. et al. (2003) Biochem. J. 373:179.
Bjelke, J.R. et al. (2006) Biochem. J. 396:391.
Ajami, K. et al. (2004) Biochim. Biophys. Acta. 1679:18.
Rosenblum, J.S. and Kozarich, J.W. et al. (2003) Curr. Opin. Chem. Biol. 7:496.
Van der Veken, P. et al. (2007) Curr. Top. Med. Chem. 7:621.
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