Recombinant Human DPPIV/CD26 (High Purity Dimer) Protein, CF Summary
Asn29-Pro766, with a C-terminal Asp-Ile 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 MES and NaCl.|
|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 DPPIV/CD26 (rhDPPIV) (Catalog # 9168-SE)
- Substrate: H-Gly-Pro-AMC (Bachem, Catalog # I-1225), 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 rhDPPIV to 0.1 ng/μL in Assay Buffer.
- Dilute Substrate to 200 μM in Assay Buffer.
- Load into a black plate 50 μL of 0.1 ng/μL rhDPPIV, and start the reaction by adding 50 μL of 200 μM Substrate. As a Substrate Blank combine 50 μL of Assay Buffer and 50 μL of 200 μM 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 # A9891).
- rhDPPIV: 0.005 μg
- Substrate: 100 μM
Recombinant Human DPPIV/CD26 (Catalog # 9168-SE) is measured by its ability to cleave the fluorogenic peptide substrate, Gly-Pro-7-amido-4-methylcoumarin (GP-AMC). The activity (orange) is approximately 4-fold greater than the competitor's DPPIV/CD26 (green).
DPPIV/CD26 (EC 184.108.40.206) is an approximately 110 kDa serine exopeptidase that releases Xaa-Pro or Xaa-Ala dipeptides from the N-terminus of oligo- and polypeptides. It regulates immune and endocrine function through the cleavage of multiple chemokines, growth factors, and peptide hormones (1, 2). Mature human DPPIV consists of a 6 amino acid (aa) cytoplasmic tail, a 22 aa transmembrane segment, and a 738 aa extracellular domain (ECD) that contains the catalytic active site (Ser, Asp, and His charge relay system) (3). Within the ECD, human DPPIV/CD26 shares 84% amino acid sequence identity with mouse and rat DPPIV. DPPIV is expressed as a noncovalent homodimer on the surface of epithelial cells, endothelial cells, and activated lymphocytes, and it can be released by MMP mediated shedding (4). It cleaves a range of peptide hormones including Glucagon, Glucagon-like Peptides 1 and 2, GIP, GHRH, Procalcitonin, Neuropeptide Y, and Substance P (5). It is released from adipocytes and induces insulin resistance in adipocytes and skeletal muscle (6). DPPIV also cleaves many chemokines, resulting in reduced chemotactic activity of CXCL6, 9, 10, 11, 12, and CCL5 (7-10) but unchanged angiostatic activity of CXCL9 and CXCL10 (8). Cleavage can increase (CCL5), decrease (CXCL12), or have no effect (CCL4) on chemokine blockade of HIV-1 cellular infectivity (7, 9, 11). In addition, DPPIV cleavage of CCL4 broadens chemokine receptor usage to also include CCR2b (11). DPPIV serves as a cell entry coreceptor for HIV and coronavirus (12, 13). It cleaves human GM-CSF and IL-3 and reduces their ability to promote myeloid cell development (14). It also interferes with CXCL12 induced hematopoietic cell migration, homing, and engraftment (15). DPPIV interacts in cis with adenosine deaminase on T cells and in trans with caveolin-1 on antigen presenting cells (16, 17). It provides costimulatory proliferation and activation signals to both CD4+ and CD8+ T cells (17, 18).
- Klemann, C. et al. (2016) Clin. Exp. Immunol. Epub PMID 26919392.
- Mortier, A. et al. (2016) J. Leukoc. Biol. Epub PMID 26744452.
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- Rohrborn, D. et al. (2014) FEBS Lett. 588:3870.
- Waumans, Y. et al. (2015) Front. Immunol. 6:387.
- Lamers, D. et al. (2011) Diabetes 60:1917.
- Proost, P. et al. (1998) J. Biol. Chem. 273:7222.
- Proost, P. et al. (2001) Blood 98:3554.
- Ohtsuki, T. et al. (1998) FEBS Lett. 431:236.
- Barreira da Silva, R. et al. (2015) Nat. Immunol. 16:850.
- Guan, E. et al. (2002) J. Biol. Chem. 277:32348.
- Callebaut, C. et al. (1993) Science 262:2045.
- Raj, V.S. et al. (2013) Nature 495:251.
- Broxmeyer, H.E. et al. (2012) Nat. Med. 18:1786.
- Christopherson II, K.W. et al. (2004) Science 305:1000.
- Kameoka, J. et al. (1993) Science 261:466.
- Ohnuma, K. et al. (2007) J. Biol. Chem. 282:10117.
- Hatano, R. et al. (2013) Immunology 138:165.
Citations for Recombinant Human DPPIV/CD26 (High Purity Dimer) 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.
Citations: Showing 1 - 9
Filter your results:
Continuous stimulation of dual-function peptide PGLP-1-VP inhibits the morbidity and mortality of NOD mice through anti-inflammation and immunoregulation
Authors: H Gao, Q Zhao, S Tang, K Li, F Qin, Z Song, Y Pan, L Jin, Y Zhang
Scientific Reports, 2021;11(1):3593.
Sample Types: Whole Cells
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.
Dipeptidyl Peptidase 4 Inhibitors Reduce Hepatocellular Carcinoma by Activating Lymphocyte Chemotaxis in Mice
Authors: S Nishina, A Yamauchi, T Kawaguchi, K Kaku, M Goto, K Sasaki, Y Hara, Y Tomiyama, F Kuribayash, T Torimura, K Hino
Cell Mol Gastroenterol Hepatol, 2019;7(1):115-134.
Sample Types: Whole Cells
Pharmacological Effects of EGLP-1, a Novel Analog of Glucagon-Like Peptide-1, on Carbohydrate and Lipid Metabolism
Authors: H Gao, Z Song, Q Zhao, Y Wu, S Tang, M Alahdal, Y Shen, Y Xing, Y Pan, J Li, Y Zhang, L Jin
Cell. Physiol. Biochem., 2018;48(3):1112-1122.
Sample Types: Whole Cells
Reduction of soluble dipeptidyl peptidase 4 levels in plasma of patients infected with Middle East respiratory syndrome coronavirus
Authors: KS Inn, Y Kim, A Aigerim, U Park, ES Hwang, MS Choi, YS Kim, NH Cho
Sample Types: Pseudotype Virus
Pericyte-targeting prodrug overcomes tumor resistance to vascular disrupting agents
Authors: M Chen, X Lei, C Shi, M Huang, X Li, B Wu, Z Li, W Han, B Du, J Hu, Q Nie, W Mai, N Ma, N Xu, X Zhang, C Fan, A Hong, M Xia, L Luo, A Ma, H Li, Q Yu, H Chen, D Zhang, W Ye
J. Clin. Invest., 2017;0(0):.
Sample Types: Recombinant Protein
Applications: Enzyme Assay
A novel recombinant antibody specific to full-length stromal derived factor-1 for potential application in biomarker studies
Authors: DI Bromage, S Taferner, M Pillai, DM Yellon, SM Davidson
PLoS ONE, 2017;12(4):e0174447.
Sample Types: Plasma
Applications: ELISA (Standard)
Improved glycaemia in high-fat-fed neprilysin-deficient mice is associated with reduced DPP-4 activity and increased active GLP-1 levels
Authors: Joshua R Willard
Characterization of the receptor-binding domain (RBD) of 2019 novel coronavirus: implication for development of RBD protein as a viral attachment inhibitor and vaccine.
Authors: Tai W, He L, Zhang X, Pu J, Voronin D, Jiang S, Zhou Y, DU L
Cell Mol Immunol, 0;17(6):613-620.
Sample Types: Whole Cells
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