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DPPIV drug discovery kit

更新時間：2022-01-28

簡要描述：

型號：廠商性質(zhì)：代理商瀏覽量：970

Measures DPPIV activity in plasma, serum, urine, and saliva
Allows correlation of DPPIV activity levels with disease states or drug treatments
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.

<strong>DPPIV drug discovery kit</strong> chart

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

Applications:	Colorimetric detection, Fluorescent detection, HTS Activity assay

Shipping:	Shipped on Dry Ice

Long Term Storage:	-80°C

Contents:	DPPIV enzyme (human, recombinant), pNA substrate, Calibration standard (p-nitroaniline), AMC substrate, Calibration standard (7-Amino-4-methylcoumarin), Inhibitor, Assay Buffer, ?-volume clear microplate

UniProt ID:	P27487

Regulatory Status:	RUO - Research Use Only

Compatibility:	This product is compatible with the Absorbance 96 Plate Reader.

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;

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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DPPIV drug discovery kit

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Product Literature References

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