Recombinant Human DPP9 Protein, CF Summary
Arg2-Leu892 with an N-terminal Met and 6-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, NaCl and Glycerol.|
|Shipping||The product is shipped with dry ice or equivalent. 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 Tris, pH 8.0
- Recombinant Human DPP9 (rhDPP9) (Catalog # 5419-SE)
- Substrate: H-Gly-Pro-AMC (Bachem, Catalog # I-1225) Prepare a 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 rhDPP9 to 1 ng/µL in Assay Buffer.
- Dilute substrate to 200 µM in Assay Buffer.
- Load 50 µL of 1 ng/µL rhDPP9 into a plate, and start the reaction by adding 50 µL of 50 µM Substrate. Include a Substrate Blank containing 50 µL of Assay Buffer and 50 µL of 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).Per Well:
- rhDPP9: 0.050 µg
- Substrate: 100 µM
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.
Citations for Recombinant Human DPP9 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.
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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, 2020-12-04;10(1):21280.
Fibroblast Activation Protein Cleaves and Inactivates Fibroblast Growth Factor 21
Authors: DR Dunshee, TW Bainbridge, NM Kljavin, J Zavala-Sol, AC Schroeder, R Chan, R Corpuz, M Wong, W Zhou, G Deshmukh, J Ly, DP Sutherlin, JA Ernst, J Sonoda
J. Biol. Chem, 2016-01-21;291(11):5986-96.
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