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D4943

Sigma-Aldrich

Dipeptidyl Peptidase IV human

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

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Synonym(s):
CD26, DPPIV, Dipeptidyl aminopeptidase IV, Glycoprotein GP110
Enzyme Commission number:
MDL number:
NACRES:
NA.54

recombinant

expressed in baculovirus infected Sf9 cells

Quality Level

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

Gene Information

human ... DPP4(1803)

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This Item
D3446D3071D3321
Dipeptidyl Peptidase IV human recombinant, expressed in baculovirus infected Sf9 cells, pkg of ≥1.0 units/vial, ≥10 units/mg protein

D4943

Dipeptidyl Peptidase IV human

Dipeptidyl Peptidase IV human recombinant, expressed in Sf9 cells

D3446

Dipeptidyl Peptidase IV human

Sigma-Aldrich

D3071

Dipeptidyl Peptidase IX human

Sigma-Aldrich

D3321

Dipeptidyl Peptidase VII human

Gene Information

human ... DPP4(1803)

Gene Information

human ... DPP4(1803)

Gene Information

-

Gene Information

-

recombinant

expressed in baculovirus infected Sf9 cells

recombinant

expressed in Sf9 cells

recombinant

expressed in Sf9 cells

recombinant

expressed in Sf9 cells

form

solution

form

solution

form

solution

form

solution

storage temp.

−20°C

storage temp.

−70°C

storage temp.

−70°C

storage temp.

−70°C

shipped in

wet ice

shipped in

dry ice

shipped in

dry ice

shipped in

dry ice

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.
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

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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DP (dipeptidyl peptidase) IV is the archetypal member of its six-member gene family. Four members of this family, DPIV, FAP (fibroblast activation protein), DP8 and DP9, have a rare substrate specificity, hydrolysis of a prolyl bond two residues from the
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