C-terminal histidine-tagged. Soluble form (residues 29-766) MW 105 kDa
Application
Human dipeptidyl peptidase IV has been used to study interactive hemodynamic effects of its inhibition and angiotensin-converting enzyme inhibition in humans. Human dipeptidyl peptidase IV has also been used in a study that informed the understanding of Hymenoptera venom allergies.
The enzyme from Sigma has been used to study the LC-MS (liquid chromatography-mass spectrometry) based assay method for DPP-IV inhibitor screening and substrate discovery.
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. The optimum pH is found to be 7.4-8.7. DPPIV is involved in the regulation of several important physiological processes such as immune functions, inflammation, CNS, endocrine functions, bone marrow mobilization, cancer growth, cell adhesion, glucose hemostasis and sepsis/severe infection.
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.
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 10 mM Tris-HCl, pH 7.6, 200 mM NaCl, 1 mM EDTA and 10% glycerol.
Other Notes
One unit will produce 1.0 μmole of p-nitroaniline from Gly-L-Pro p-nitroanilide per min in 100 mM Tris-HCl at pH 7.6 at 37 °C.
The specification is that each vial will be provided at a concentration of ≥10ug protein/mL, and that the activity will be ≥ 10units per mg protein. The calculations to make a solution of 0.005U/mL will be dependent on the specific activity of the lot.
Helpful?
·a year ago
이 효소 제품은 Gly-Pro p-nitroanilide만을 분해할 수 있나요? D3446의 Specification Sheet에는 Ala-Pro-AMC를 분해한다고 나와 있는데, D4943은 Gly-Pro p-nitroanilide만을 분해할 수 있고 D3446은 Ala-Pro-AMC만을 분해할 수 있는건지 알고싶습니다.
1 answer
Technical Support
·a year ago
As described above, 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. pNA (p-nitroanilide) and AMC (7-amino-4-methylcoumarin) are substrate conjugates that are used for the quantitative analysis of enzyme activities by chromogenic or fluorogenic detection, respectively.