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D7052

Dipeptidyl Peptidase IV from porcine kidney

lyophilized powder, ≥10 units/mg protein (Bradford)

Synonym(e):

Dipeptidyl aminopeptidase IV

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Über diesen Artikel

CAS-Nummer:
EG-Nummer:
UNSPSC Code:
12352204
MDL number:


form

lyophilized powder

specific activity

≥10 units/mg protein (Bradford)

mol wt

124 kDa

packaging

vial of ≥0.75 unit

solubility

0.1 M Tris-HCl, pH 8.0: soluble 1 vial/mL, clear, colorless

UniProt accession no.

storage temp.

−20°C

Gene Information

pig ... DPPIV(397492)

Application

Dipeptidyl peptidase IV from porcine kidney has been used in a study to investigate engraftment of donor cells following hepatocyte transplantation. Dipeptidyl peptidase IV from porcine kidney has also been used in a study to investigate the metabolism of glucagon-like peptide-2.
The enzyme from sigma has been used in the determination of DPP-IV inhibitory activity of peptides in porcine skin gelatin hydrolysates.

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. 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.
The pH optimum for the protease is 7.8-8.0. Dipeptidyl peptidase does not require activators. It is inhibited by diisopropyl fluorophosphate, phenylmethanesulfonyl fluoride, and diethyl p-nitrophenyl phosphate.[1][2]

Physical form

Lyophilized powder containing Tris buffer salts

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 8.0 at 37 °C.


pictograms

Health hazardExclamation mark

signalword

Danger

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Lagerklasse

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Gloves



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Verwandter Inhalt

Product Information Sheet


Dipeptidyl Peptidase-IV Inhibitory Activity of Peptides in Porcine Skin Gelatin Hydrolysates.
Hsu, Kuo-Chiang, et al.
Bioactive Food Peptides in Health and Disease, 205-205 (2013)
Kosho Yamanouchi et al.
Hepatology (Baltimore, Md.), 49(1), 258-267 (2008-11-13)
Engraftment of donor hepatocytes is a critical step that determines the success of hepatocyte transplantation. Rapid and efficient integration of donor cells would enable prompt liver repopulation of these cells in response to selective proliferative stimuli offered by a preparative
A J Kenny et al.
The Biochemical journal, 157(1), 169-182 (1976-07-01)
Dipeptidyl peptidase IV, an enzyme that releases dipeptides from substrates with N-terminal sequences of the forms X-Pro-Y or X-Ala-Y, was purified 300-fold from pig kidney cortex. The kidney is the main source of the enzyme, where it is one of