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D3446

Sigma-Aldrich

Dipeptidyl Peptidase IV human

recombinant, expressed in Sf9 cells

Synonyme(s) :

CD26, DPPIV, Dipeptidyl aminopeptidase IV, Glycoprotein GP110

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About This Item

Numéro de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Produit recombinant

expressed in Sf9 cells

Niveau de qualité

Forme

solution

Activité spécifique

≥4,000 units/μg protein

Poids mol.

124 kDa

Concentration

≥0.01 mg/mL

Numéro d'accès UniProt

Maladie(s) pertinente(s)

cancer (lymphoma, prostate and colon cancer)

Conditions d'expédition

dry ice

Température de stockage

−70°C

Informations sur le gène

human ... DPP4(1803)

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Catégories apparentées

Description générale

Dipeptidyl Peptidase IV (DPP4) is mapped to human chromosome 2q24.2. It comprises the N-glycosylation sites located in the β-propeller domain.

Application

Dipeptidyl Peptidase IV human has been used in DPP-IV inhibitory activity assay of quinoa protein concentrate digest.
Human dipeptidyl peptidase IV has been used in a study to assess the interactive hemodynamic effects of its inhibition as well as the angiotensin-converting enzyme inhibition. Human dipeptidyl peptidase IV has also been used in a study to identify and characterize the 100 kDa High Molecular Weight Hymenoptera Venom Allergens Api m 5 and Ves v 3.

Actions biochimiques/physiologiques

Dipeptidyl Peptidase IV (DPP4) mediates the activation of T-cells. It is also a potential biomarker for lymphoma, thyroid, prostate and colon cancer.
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 hydrolyze 1.0 picomole of Ala-Pro-AMC per minute at pH 7.5 at 25 deg °C

Forme physique

Supplied as a solution in 45 mM Tris-HCl, pH 8.0, 124 mM NaCl, 2.4 mM KCl, 225 mM imidazole and 10% glycerol.

Autres remarques

Pictogrammes

Health hazardExclamation mark

Mention d'avertissement

Danger

Mentions de danger

Classification des risques

Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2

Code de la classe de stockage

6.1D - Non-combustible acute toxic Cat.3 / toxic hazardous materials or hazardous materials causing chronic effects

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

N-linked glycosylation of dipeptidyl peptidase IV (CD26): Effects on enzyme activity, homodimer formation, and adenosine deaminase binding
Aertgeerts K, et al.
Protein Science, 13(1), 145-154 (2004)
Unravelling the immunological roles of dipeptidyl peptidase 4 (DPP4) activity and/or structure homologue (DASH) proteins
Wagner L, et al.
Clinical and Experimental Immunology, 184(3), 265-283 (2016)
Junkun Pan et al.
Frontiers in nutrition, 9, 892426-892426 (2022-06-01)
With the aim to establish a structure-inhibitory activity relationship of flavonoids against dipeptidyl peptidase-4 (DPP-4) and elucidate the interaction mechanisms between them, a pannel of 70 structurally diverse flavonoids was used to evaluate their inhibitory activities against DPP-4, among which
Release of dipeptidyl peptidase IV, alpha-amylase and alpha-glucosidase inhibitory peptides from quinoa (Chenopodium quinoa Willd.) during in vitro simulated gastrointestinal digestion
Vilcacundo R, et al.
Journal of functional foods, 35, 531-539 (2017)
Annis Marney et al.
Hypertension (Dallas, Tex. : 1979), 56(4), 728-733 (2010-08-04)
Dipeptidyl peptidase-IV inhibitors improve glucose homeostasis in type 2 diabetics by inhibiting degradation of the incretin hormones. Dipeptidyl peptidase-IV inhibition also prevents the breakdown of the vasoconstrictor neuropeptide Y and, when angiotensin-converting enzyme (ACE) is inhibited, substance P. This study

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