D7052
Dipeptidyl Peptidase IV from porcine kidney
lyophilized powder, ≥10 units/mg protein (Bradford)
Synonyme(s) :
Dipeptidyl aminopeptidase IV
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About This Item
Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352204
Produits recommandés
Forme
lyophilized powder
Activité spécifique
≥10 units/mg protein (Bradford)
Poids mol.
124 kDa
Conditionnement
vial of ≥0.75 unit
Solubilité
0.1 M Tris-HCl, pH 8.0: soluble 1 vial/mL, clear, colorless
Numéro d'accès UniProt
Température de stockage
−20°C
Informations sur le gène
pig ... DPPIV(397492)
Spécificité
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.
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.[1]
Actions biochimiques/physiologiques
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.
Définition de l'unité
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.
Forme physique
Lyophilized powder containing Tris buffer salts
Inhibiteur
Substrat
Réf. du produit
Description
Tarif
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Organes cibles
Respiratory system
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
dust mask type N95 (US), Eyeshields, Gloves
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Les clients ont également consulté
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)
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
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
K M Fukasawa et al.
Biochimica et biophysica acta, 657(1), 179-189 (1981-01-15)
Dipeptidyl peptidase IV (dipeptidylpeptide hydrolase, EC 3.4.14.-) has been purified from the microsomal fraction of pig liver, using an immunoaffinity chromatography, and its properties compared with those of the enzyme purified from pig kidney. The amino acid compositions of both
Thi Thu Huong Do et al.
American journal of physiology. Endocrinology and metabolism, 306(6), E668-E680 (2014-01-16)
The oligopeptide transporter peptide cotransporter-1 Slc15a1 (PEPT1) plays a major role in the regulation of nitrogen supply, since it is responsible for 70% of the dietary nitrogen absorption. Previous studies demonstrated that PEPT1 expression and function in jejunum are reduced
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