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Measures DPPIV activity in plasma, serum, urine, and saliva
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Allows correlation of DPPIV activity levels with disease states or drug treatments
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Allows determination of efficacy of DPPIV inhibitors
The DPPIV Drug Discovery Kit is a complete assay system designed to screen DPPIV inhibitors, providing enough material to perform at least 96 assays. DPPIV (DPP4, CD26) is a member of the class of proteases known as prolyl peptidases, which cleave proteins after proline residues and is thought to play roles in diabetes, cancer, and autoimmune diseases, making it a target for drug discovery.
The kit contains both a chromogenic substrate (H-Gly-Pro-pNA; Km=114 µM) and a fluorogenic substrate (H-Gly-Pro-AMC; Km=50 µM).
Cleavage of the p-nitroaniline (pNA) from the colorimetric substrate increases absorbance at 405 nm. The fluorimetric assay is based on the cleavage of 7-amino-4-methylcoumarin (AMC) moiety from the C-terminus of the peptide substrate, which increases its fluorescence intensity at 460 nm. The kit is useful to screen inhibitors of DPPIV, a potential therapeutic target. A DPPIV inhibitor, P32/98 (KI=130 nM12), is included for use as a control. Other DPP enzymes are available for specificity profiling.
Plot data as Relative Fluorescence Units (RFU) versus time for each sample.
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Product Details
Alternative Name: | CD26, Dipeptidyl Peptidase IV, DPP4 |
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Applications: | Colorimetric detection, Fluorescent detection, HTS Activity assay
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Shipping: | Dry Ice |
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Long Term Storage: | -80°C |
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Contents: | DPPIV enzyme (human, recombinant), pNA substrate, Calibration standard (p-nitroaniline), AMC substrate, Calibration standard (7-Amino-4-methylcoumarin), Inhibitor, Assay Buffer, ½-volume clear microplate |
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UniProt ID: | P27487 |
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Regulatory Status: | RUO - Research Use Only |
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Compatibility: | This product is compatible with the Absorbance 96 Plate Reader.
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Product Literature References
Semi-Industrial Production of a DPP-IV and ACE Inhibitory Peptide Fraction from Whey Protein Concentrate Hydrolysate by Electrodialysis with Ultrafiltration Membrane: M. Faucher, et al.; Membranes
12, 409 (2022),
Abstract;
Transcriptome profiling of two Moringa species and insights into their antihyperglycemic activity: K.M. Shafi, et al.; BMC Plant Biol.
22, 561 (2022),
Abstract;
Study on the Mechanism of the Blood-Glucose-Lowering Effect of Collagen Peptides from Sturgeon By-Products: Y. Sasaoka, et al.; Mar. Drugs
19, 584 (2021),
Abstract;
Sitagliptin decreases ventricular arrhythmias by attenuated glucose-dependent insulinotropic polypeptide (GIP)-dependent resistin signaling in infarcted rats: T.M. Lee, et al.; Biosci. Rep.
36, e00307 (2016),
Application(s): Measurement of Dpp-4 levels in plasma,
Abstract;
Full Text
Comparison of the susceptibility of porcine and human dipeptidyl-peptidase IV to inhibition by protein-derived peptides: I.M. Lacroix, et al.; Peptides
69, 19 (2015),
Application(s): Assay,
Abstract;
Novel N-substituted aminobenzamide scaffold derivatives targeting the dipeptidyl peptidase-IV enzyme: Q.A. Al-Balas, et al. ; Drug Des. Devel. Ther.
8, 129 (2014),
Application(s): Assay,
Abstract;
Full Text
The dipeptidyl peptidase-4 inhibitor Saxagliptin improves function of circulating pro-angiogenic cells from type 2 diabetic patients: N. Poncina, et al.; Cardiovasc. Diabetol.
13, 92 (2014),
Abstract;
Full Text
16, 17-Dihydro-17b-hydroxy isomitraphylline alkaloid as an inhibitor of DPP-IV, and its effect on incretin hormone and β-cell proliferation in diabetic rat: A. Shukla, et al.; Eur. J. Pharm.
47, 512 (2012),
Application(s): Measurement of inhibition of DPPIV by DHIM,
Abstract;
Identification of diverse dipeptidyl peptidase IV inhibitors via structure-based virtual screening: C. Li, et al.; J. Mol. Model
18, 4033 (2012),
Abstract;
Synthesis, structure-activity relationship, and pharmacophore modeling studies of pyrazole-3-carbohydrazone derivatives as dipeptidyl peptidase IV inhibitors: D. Wu, et al.; Chem. Biol. Drug Des.
79, 897 (2012),
Abstract;
Discovery and preclinical profile of Saxagliptin (BMS-477118): a highly potent, long-acting, orally active dipeptidyl peptidase IV inhibitor for the treatment of type 2 diabetes: D. J. Augeri et al.; J. Med. Chem.
48, 5025 (2005),
Abstract;
CD26/dipeptidyl peptidase IV and its role in cancer: B. et al.; Histol. Histopathol.
19, 1345 (2004),
Abstract;
CD26/dipeptidyl peptidase IV: a regulator of immune function and a potential molecular target for therapy: U. Aytac et al.; Curr. Drug. Targets Immune Endocr. Metabol. Disord.
4, 11 (2004),
Abstract;
Dipeptidyl peptidase IV inhibitors for the treatment of diabetes: A. E. Weber et al.; J. Med. Chem.
47, 4135 (2004),
Abstract;
N-linked glycosylation of dipeptidyl peptidase IV (CD26): effects on enzyme activity, homodimer formation, and adenosine deaminase binding: K. Aertgeerts et al.; Protein Sci.
13, 145 (2004),
Abstract;
Dipeptidyl peptidase IV (CD26) activity in the hematopoietic system: differences between the membrane-anchored and the released enzyme activity: D. A. Pereira et al.; Braz. J. Med. Biol. Res.
36, 567 (2003),
Abstract;
Dipeptidyl peptidase IV inhibitor treatment stimulates beta-cell survival and islet neogenesis in streptozotocin-induced diabetic rats: J. A. Pospisilik et al.; Diabetes
52, 741 (2003),
Abstract;
Prolyl peptidases: a serine protease subfamily with high potential for drug discovery: J. S. Rosenblum et al.; Curr. Opin. Chem. Biol.
7, 496 (2003),
Abstract;
Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV: R. Thoma et al.; Structure
11, 947 (2003),
Abstract;
On the regulatory role of dipeptidyl peptidase IV (=CD=adenosine deaminase complexing protein) on adenosine deaminase activity: I. Ben-Shooshan; Biochim. Biophys. Acta.
1587, 21 (2002),
Abstract;
Human serum dipeptidyl peptidase IV (DPPIV) and its unique properties: H. Shibuya-Saruta; J. Clin. Lab. Anal.
10, 435 (1996),
Abstract;
Activity of dipeptidyl peptidase IV and post-proline cleaving enzyme in sera from osteoporotic patients: H. Gotoh et al.; Clin. Chem.
34, 2499 (1988),
Abstract;
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