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DPPIV drug discovery kit

BML-AK499-0001 96 wells 324.00 USD
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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.

Product Specification

Alternative Name:CD26, Dipeptidyl Peptidase IV, DPP4
Applications:Colorimetric detection, Fluorescent detection, HTS
Activity assay
Shipping:Shipped on Dry Ice
Long Term Storage:-80°C
Kit/Set Contains: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
UniProt ID:P27487

Product Literature References

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;
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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