DPRP2 (dipeptidyl peptidase IV-related protein-2), also called DPP9 (dipeptidyl-peptidase 9), is a soluble cytoplasmic prolyl-peptidase, which is not well characterized. It is a proline cleaving peptidase, which belongs to the S9B/ DPPIV family. It is an exopeptidase, which cleaves off dipeptides from proteins at the second proline (Xaa-Pro) on the N-terminal side. In vertebrates it is ubiquitously expressed, and shares 60% sequence similarity with DPP8.
Immunogen
Immunogen Sequence: GI # 21040237, sequence 426-519
Anti-DPRP2 antibody produced in chicken is suitable for western blotting analysis at a dilution of 1:500, for tissue or cell staining at a dilution of 1:200.
Biochem/physiol Actions
Dipeptidyl peptidase 9 is involved in various cellular pathways including amino acid recycling, antigen maturation, cellular homeostasis, and viability. DPP9 plays an important role in the regulation of survival and proliferation pathways. It also plays a crutial role in peptide turnover and antigen presentation. DPP9 have unique peptidase and extra-enzymatic activities that have been implicated in various diseases including cancers.
Physical form
Solution in phosphate buffered saline containing 0.02% sodium azide.
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The amino terminus extension in the long dipeptidyl peptidase 9 isoform contains a nuclear localization signal targeting the active peptidase to the nucleus.
Justa-Schuch D, Moller U, and Geiss-Friedlander R
Cellular and Molecular Life Sciences, 71(18), 3611-3626 (2014)
The Journal of biological chemistry, 284(40), 27211-27219 (2009-08-12)
Protein degradation is an essential process that continuously takes place in all living cells. Regulated degradation of most cellular proteins is initiated by proteasomes, which produce peptides of varying length. These peptides are rapidly cleaved to single amino acids by
Molecular cancer research : MCR, 9(7), 948-959 (2011-05-31)
Dipeptidyl peptidase IV (DPP4), DPP8, DPP9, and fibroblast activation protein (FAP), the four proteases of the DPP4 gene family, have unique peptidase and extra-enzymatic activities that have been implicated in various diseases including cancers. We report here a novel role
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