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
• EC Number: 3.4.14.5 (BRENDA, IUBMB)
• MDL number: MFCD00166456
• UNSPSC Code: 12352204
• NACRES: NA.54

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.

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.

Unit Definition

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.

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

View more information on Dipeptidyl Peptidase IV at www.sigma-aldrich.com/enzymeexplorer.

Safety Information

• Storage Class Code: 10 - Combustible liquids
• WGK: WGK 1
• Flash Point(F): Not applicable
• Flash Point(C): Not applicable