D4943
Dipeptidyl Peptidase IV human
recombinant, expressed in baculovirus infected Sf9 cells, pkg of ≥1.0 units/vial, ≥10 units/mg protein
Synonyme(s) :
CD26, DPPIV, Dipeptidyl aminopeptidase IV, Glycoprotein GP110
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A propos de cet article
Specific activity:
≥10 units/mg protein
Recombinant:
expressed in baculovirus infected Sf9 cells
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Laissez-nous vous aiderrecombinant
expressed in baculovirus infected Sf9 cells
form
solution
specific activity
≥10 units/mg protein
mol wt
105 kDa
packaging
pkg of ≥1.0 units/vial
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
Quality Level
Gene Information
human ... DPP4(1803)
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General description
C-terminal histidine-tagged. Soluble form (residues 29-766) MW 105 kDa
Application
Human dipeptidyl peptidase IV has been used to study interactive hemodynamic effects of its inhibition and angiotensin-converting enzyme inhibition in humans. Human dipeptidyl peptidase IV has also been used in a study that informed the understanding of Hymenoptera venom allergies.
The enzyme from Sigma has been used to study the LC-MS (liquid chromatography-mass spectrometry) based assay method for DPP-IV inhibitor screening and substrate discovery.
Biochem/physiol Actions
DPPIV has a post-proline dipeptidyl aminopeptidase activity that hydrolyzes N-terminal dipeptides from the unsubstituted N-terminus of peptides with the sequence of X-Pro-Z and X-Ala-Z. The optimum pH is found to be 7.4-8.7. DPPIV is involved in the regulation of several important physiological processes such as immune functions, inflammation, CNS, endocrine functions, bone marrow mobilization, cancer growth, cell adhesion, glucose hemostasis and sepsis/severe infection.
DPPIV has a post-proline dipeptidyl aminopeptidase activity that hydrolyzes N-terminal dipeptides from the unsubstituted N-terminus of peptides with the sequence of X-Pro-Z and X-Ala-Z. Where X is a nonspecific residue at the N terminus and Z cannot be proline or hydroxyproline.
Native DPPIV is a ubiquitous type II transmembrane glycoprotein and a serine protease of the S9 prolyl-oligopeptidase family. In vivo, it is synthesized with a signal peptide, which functions as the membrane anchoring domain. There is an 88% sequence homology between the human and porcine kidney enzymes. Both exist as homodimers with a subunit molecular weight of ~30 kDa. The high mannose 100 kDa DPPIV precursor is processed in the Golgi to yield a 124 kDa heavily N-and O-linked mature glycoprotein. It is then sorted to the apical membrane through the concerted action of both N- and O-linked glycans and its association with lipid microdomains. The porcine enzyme contains 18.3% carbohydrates, which the glycan composition is 0.9% fucose, 3.4% mannose, 5.1% galactose, 8.2% glucosamine, and 0.7% sialic acid. DPPIV is highly expressed on endothelial cells, epithelial cells, and lymphocytes. It is also present in plasma in its soluble form.
Physical form
Supplied as a solution in 10 mM Tris-HCl, pH 7.6, 200 mM NaCl, 1 mM EDTA and 10% glycerol.
Other Notes
One unit will produce 1.0 μmole of p-nitroaniline from Gly-L-Pro p-nitroanilide per min in 100 mM Tris-HCl at pH 7.6 at 37 °C.
View more information on Dipeptidyl Peptidase IV at www.sigma-aldrich.com/enzymeexplorer.
Classe de stockage
10 - Combustible liquids
flash_point_f
Not applicable
flash_point_c
Not applicable
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Scientific reports, 12(1), 9100-9100 (2022-06-02)
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Ivan O Maslov et al.
Pharmaceuticals (Basel, Switzerland), 15(3) (2022-03-27)
Compounds that contain (R)-3-amino-4-(2,4,5-trifluorophenyl)butanoic acid substituted with bicyclic amino moiety (2-aza-bicyclo[2.2.1]heptane) were designed using molecular modelling methods, synthesised, and found to be potent DPP-4 (dipeptidyl peptidase-4) inhibitors. Compound 12a (IC50 = 16.8 ± 2.2 nM), named neogliptin, is a more
Ryugen Takahashi et al.
Frontiers in oncology, 11, 714527-714527 (2021-09-08)
Radical resection is the only curative treatment for pancreatic cancer, which is a life-threatening disease. However, it is often not easy to accurately identify the extent of the tumor before and during surgery. Here we describe the development of a
LC-MS based assay method for DPP-IV inhibitor screening and substrate discovery.
Liu, J., Cheng, X., & Fu, L.
Analytical Methods : Advancing Methods and Applications, 4(6), 1797-1805 (2012)
Annis Marney et al.
Hypertension (Dallas, Tex. : 1979), 56(4), 728-733 (2010-08-04)
Dipeptidyl peptidase-IV inhibitors improve glucose homeostasis in type 2 diabetics by inhibiting degradation of the incretin hormones. Dipeptidyl peptidase-IV inhibition also prevents the breakdown of the vasoconstrictor neuropeptide Y and, when angiotensin-converting enzyme (ACE) is inhibited, substance P. This study
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