Recombinant Human DPPII/QPP/DPP7 Protein, CF

Catalog # Availability Size / Price Qty
3438-SE-010
R&D Systems Recombinant Proteins and Enzymes
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Citations (3)
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Recombinant Human DPPII/QPP/DPP7 Protein, CF Summary

Product Specifications

Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
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, Lys-Pro-AMC (KP-AMC). The specific activity is >4,000 pmol/min/µg, as measured under the described conditions.
Source
Mouse myeloma cell line, NS0-derived human DPPII/QPP/DPP7 protein
Gly22-Leu492, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Analysis
Gly22 & Arg24
Predicted Molecular Mass
54 kDa
SDS-PAGE
64 kDa, reducing conditions

Product Datasheets

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3438-SE

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.

3438-SE

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.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.

Assay Procedure

Materials
  • 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
  1. Dilute rhDPP7 to 0.2 ng/µL in Assay Buffer.
  2. Dilute Substrate to 200 µM in Assay Buffer.
  3. 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.
  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:
  • rhDPP7: 0.01 µg
  • Substrate: 100 µM
Reconstitution Calculator

Reconstitution Calculator

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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.

References
  1. Underwood, R. et al. (1999) J. Biol. Chem. 274:34053.
  2. Maes, M.B. et al. (2005) Biochem. J. 386:315.
  3. Rosenblum, J.S. and J.W. Kozarich (2003) Curr. Opin. Chem. Biol. 7:496.
  4. Lankas, G.R. et al. (2005) Diabetes 54:2988.
Long Name
Dipeptidyl-peptidase II
Entrez Gene IDs
29952 (Human); 83768 (Mouse); 83799 (Rat)
Alternate Names
carboxytripeptidase; Dipeptidyl aminopeptidase II; dipeptidyl arylamidase II; dipeptidyl peptidase 2; Dipeptidyl peptidase 7; Dipeptidyl peptidase II; dipeptidylpeptidase 7; dipeptidyl-peptidase 7; dipeptidyl-peptidase II; DPP II; DPP2; DPP7; DPPII; EC 3.4.14.2; QPP; Quiescent cell proline dipeptidase

Citations 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.

3 Citations: Showing 1 - 3
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  1. Tumoral acidosis promotes adipose tissue depletion by fostering adipocyte lipolysis
    Authors: Lefevre, C;Thibaut, MM;Loumaye, A;Thissen, JP;Neyrinck, AM;Navez, B;Delzenne, NM;Feron, O;Bindels, LB;
    Molecular metabolism
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  2. 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
  3. 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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