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Recombinant Human DPP9 Protein, CF

Catalog #: 5419-SE
2 Citations Datasheet / COA / SDS
Catalog # Availability Size / Price Qty
5419-SE-010
R&D Systems Recombinant Proteins and Enzymes
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Product Details
Citations (2)
FAQs
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Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Human DPP9 Protein, CF Summary

Product Specifications

Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<1.0 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its ability to cleave the fluorogenic peptide substrate, Gly-Pro-7-amido-4-methylcoumarin (GP-AMC). The specific activity is >750 pmol/min/μg, as measured under the described conditions.
Source
Spodoptera frugiperda, Sf 21 (baculovirus)-derived human DPP9 protein
Arg2-Leu892 with an N-terminal Met and 6-His tag
Accession #
Q1ZZB8
N-terminal Sequence
Analysis
No result obtained
Predicted Molecular Mass
101 kDa
SDS-PAGE
92 kDa, reducing conditions

Product Datasheets

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5419-SE

Product Datasheet
COA
SDS

Carrier Free

What does CF mean?

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.

What formulation is right for me?

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.

5419-SE

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.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.

Assay Procedure

Materials
  • 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
  1. Dilute rhDPP9 to 1 ng/µL in Assay Buffer.
  2. Dilute substrate to 200 µM in Assay Buffer.
  3. 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.
  4. Read at excitation and emission wavelengths of 380 nm and 460 nm, respectively in kinetic mode for 5 minutes.
  5. 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
Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: DPP9

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).

References
  1. Olsen, C. and Wagtmann, N. (2002) Gene 299:185.
  2. Qi, S.Y. et al. (2003) Biochem. J. 373:179.
  3. Bjelke, J.R. et al. (2006) Biochem. J. 396:391.
  4. Ajami, K. et al. (2004) Biochim. Biophys. Acta. 1679:18.
  5. Rosenblum, J.S. and Kozarich, J.W. et al. (2003) Curr. Opin. Chem. Biol. 7:496.
  6. Van der Veken, P. et al. (2007) Curr. Top. Med. Chem. 7:621.
Long Name
Dipeptidyl peptidase 9
Entrez Gene IDs
91039 (Human); 224897 (Mouse); 301130 (Rat)
Alternate Names
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

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.

2 Citations: Showing 1 - 2
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  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, 2020-12-04;10(1):21280.
    Species: N/A
    Sample Types:
    Applications: Bioassay
  2. 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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