Human DPPII/QPP/DPP7 Antibody Summary
Gly22-Leu492
Accession # AAH11907
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: DPPII/QPP/DPP7
Dipeptidyl-peptidase II (DPPII) is identical to quiescent cell proline dipeptidase (QPP) and dipeptidylpeptidase 7 (DPP7) (1, 2). It shares some substrate and cleavage specificity with DPPIV/CD26, DPP8, DPP9 and seprase/FAP (fibroblast activation protein), members of the S09 family of serine proteases. As prolyl proteases that cleave proteins and peptides after proline residues, these enzymes have high potential for drug discovery (3, 4). However, DPP7 is not a member of the S09 family, but a member of the S28 family that also includes lysosomal Pro‑X carboxypeptidase/prolylcarboxypeptidase/PRCP and thymus-specific serine peptidase/PRSS16 (2). The human DPP7 precursor consists of a signal peptide (aa 1‑21) and a mature chain (aa 22‑492). The purified rhDPP7 is active against Lys-Pro-AMC and Lys‑Ala‑AMC. Its activity against Lys-Pro-AMC is approximately 10-fold of that against Lys-Ala-AMC under otherwise identical conditions.
- Underwood, R. et al. (1999) J. Biol. Chem. 274:34053.
- Maes, M.B. et al. (2005) Biochem. J. 386:315.
- Rosenblum, J.S. and J.W. Kozarich (2003) Curr. Opin. Chem. Biol. 7:496.
- Lankas, G.R. et al. (2005) Diabetes 54:2988.
Product Datasheets
Citation for Human DPPII/QPP/DPP7 Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
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HAO1-mediated oxalate metabolism promotes lung pre-metastatic niche formation by inducing neutrophil extracellular traps
Authors: Zhicheng Zeng, Shaowan Xu, Feifei Wang, Xin Peng, Wanning Zhang, Yizhi Zhan et al.
Oncogene
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