D3446
Dipeptidyl Peptidase IV human
recombinant, expressed in Sf9 cells
Synonym(s):
CD26, DPPIV, Dipeptidyl aminopeptidase IV, Glycoprotein GP110
recombinant
expressed in Sf9 cells
Quality Level
form
solution
specific activity
≥4,000 units/μg protein
mol wt
124 kDa
concentration
≥0.01 mg/mL
UniProt accession no.
relevant disease(s)
cancer (lymphoma, prostate and colon cancer)
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... DPP4(1803)
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General description
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.
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.
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.
Physical form
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.
Other Notes
One unit will hydrolyze 1.0 picomole of Ala-Pro-AMC per minute at pH 7.5 at 25 deg °C
View more information on Dipeptidyl Peptidase IV at www.sigma-aldrich.com/enzymeexplorer.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2
Storage Class Code
6.1D - Non-combustible acute toxic Cat.3 / toxic hazardous materials or hazardous materials causing chronic effects
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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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)
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
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
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