D4943

Dipeptidyl Peptidase IV human

recombinant, expressed in baculovirus infected Sf9 cells, pkg of ≥1.0 units/vial, ≥10 units/mg protein

• Synonym(s): CD26, DPPIV, Dipeptidyl aminopeptidase IV, Glycoprotein GP110
• UNSPSC Code: 12352204
• NACRES: NA.54
• EC Number: 3.4.14.5 (BRENDA, IUBMB)
• MDL number: MFCD00166456
• Specific activity: ≥10 units/mg protein
• Recombinant: expressed in baculovirus infected Sf9 cells

Properties

• recombinant: expressed in baculovirus infected Sf9 cells
• Quality Level: 200
• form: solution
• specific activity: ≥10 units/mg protein
• mol wt: 105 kDa
• packaging: pkg of ≥1.0 units/vial
• UniProt accession no.: P27487
• shipped in: wet ice
• storage temp.: −20°C
• Gene Information: human ... DPP4(1803)

Description

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.[1][2][3]

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.

Safety Information

• Storage Class: 10 - Combustible liquids
• flash_point_f: Not applicable
• flash_point_c: Not applicable