D3446
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 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
View more information on Dipeptidyl Peptidase IV at www.sigma-aldrich.com/enzymeexplorer.
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
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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Les clients ont également consulté
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)
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)
Simon Blank et al.
Journal of immunology (Baltimore, Md. : 1950), 184(9), 5403-5413 (2010-03-30)
Insect stings can cause life-threatening IgE-mediated anaphylactic reactions in venom-allergic patients. Although several compounds have already been described as venom allergens, prominent allergen candidates especially in the higher m.w. range have still remained elusive. Tandem mass spectrometry-based sequencing assigned a
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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