Recombinant Human DPPII/QPP/DPP7 Protein, CF Summary
Gly22-Leu492, with a C-terminal 10-His tag
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Supplied as a 0.2 μm filtered solution in Tris and NaCl.|
|Shipping||The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
- Assay Buffer: 25 mM MES, pH 6.0
- Recombinant Human DPPII/QPP/DPP7 (rhDPP7) (Catalog # 3438-SE)
- Substrate Lys-Pro-AMC (Bachem, Catalog # I-1745), 10 mM stock in DMSO
- F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
- Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
- Dilute rhDPP7 to 0.2 ng/µL in Assay Buffer.
- Dilute Substrate to 200 µM in Assay Buffer.
- Load into a black microplate 50 µL of 0.2 ng/µL rhDPP7, and start the reaction by adding 50 μL of 200 µM Substrate. Include a Substrate Blank containing Assay Buffer in place of rhDPP7 and Substrate.
- Read at excitation and emission wavelengths of 380 nm and 460 nm, respectively, in kinetic mode for 5 minutes.
- Calculate specific activity:
Specific Activity (pmol/min/µg) =
|Adjusted Vmax* (RFU/min) x Conversion Factor** (pmol/RFU)|
|amount of enzyme (µg)|
*Adjusted for Substrate Blank
**Derived using calibration standard 7-amino, 4-Methyl Coumarin (Sigma, Catalog # A-9891)
- rhDPP7: 0.01 µg
- Substrate: 100 µM
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.
Citation for Recombinant Human DPPII/QPP/DPP7 Protein, CF
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
Discovery of a novel fibroblast activation protein (FAP) inhibitor, BR103354, with anti-diabetic and anti-steatotic effects
Authors: JM Cho, EH Yang, W Quan, EH Nam, HG Cheon
Scientific Reports, 2020;10(1):21280.
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