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Merck

D3446

Sigma-Aldrich

Dipeptidyl Peptidase IV human

recombinant, expressed in Sf9 cells

Sinónimos:

CD26, DPPIV, Dipeptidyl aminopeptidase IV, Glycoprotein GP110

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About This Item

Comisión internacional de enzimas:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54

recombinante

expressed in Sf9 cells

Nivel de calidad

formulario

solution

actividad específica

≥4,000 units/μg protein

mol peso

124 kDa

concentración

≥0.01 mg/mL

Nº de acceso UniProt

enfermedades relevantes

cancer (lymphoma, prostate and colon cancer)

Condiciones de envío

dry ice

temp. de almacenamiento

−70°C

Información sobre el gen

human ... DPP4(1803)

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Descripción general

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

Aplicación

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.

Acciones bioquímicas o fisiológicas

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.

Definición de unidad

One unit will hydrolyze 1.0 picomole of Ala-Pro-AMC per minute at pH 7.5 at 25 deg °C

Forma física

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.

Otras notas

Pictogramas

Health hazardExclamation mark

Palabra de señalización

Danger

Frases de peligro

Clasificaciones de peligro

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

Código de clase de almacenamiento

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

Clase de riesgo para el agua (WGK)

WGK 1

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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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)
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)
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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