D3446
Dipeptidyl Peptidase IV human
recombinant, expressed in Sf9 cells
Synonym(s):
CD26, DPPIV, Dipeptidyl aminopeptidase IV, Glycoprotein GP110
Product Name
Dipeptidyl Peptidase IV human, recombinant, expressed in Sf9 cells
recombinant
expressed in Sf9 cells
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
Quality Level
Gene Information
human ... DPP4(1803)
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Related Categories
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.
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.
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.
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.
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2
Storage Class
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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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)
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
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)
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
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