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D4943 Sigma

Dipeptidyl Peptidase IV human

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

Synonym: CD26, DPPIV, Dipeptidyl aminopeptidase IV, Glycoprotein GP110



Related Categories 3.4.x.x Peptidases, 3.x.x.x Hydrolases, Biochemicals and Reagents, Dipeptidyl peptidase IV, Enzyme Class Index,
recombinant   expressed in baculovirus infected Sf9 cells
assay   ≥10 units/mg protein
packaging   pkg of ≥1.0 units/vial
shipped in   wet ice
storage temp.   −20°C
Gene Information   human ... DPP4(1803)


General description

C-terminal histidine-tagged. Soluble form (residues 29-766) MW 105 kDa

Other Notes

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

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.


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.

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.

Price and Availability

Biomedical Applications
Safety & Documentation

Safety Information

NONH for all modes of transport
WGK Germany 


Certificate of Analysis

Certificate of Origin

Protocols & Articles


Plasma Derived Proteins and Enzymes

Despite their complexity, blood and plasma are abundant biological resources for the discovery of drug targets and biomarkers for human disease. It is estimated that plasma may contain as many as 40,...
BioFiles 2006, 1.5, 2.
Keywords: Applications, Gas chromatography, Type

Related Content

Enzymes & Proteins

Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Molecular biology

Peer-Reviewed Papers


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