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DIPEPTIDYL PEPTIDASE IV
Кат. №: D4943-1VL
Производитель: Sigma-Aldrich
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DIPEPTIDYL PEPTIDASE IV
Main image
Кат. №: D4943-1VL
Производитель: Sigma-Aldrich
Кол-во:
Фасовка:
Цена по запросу
Товар оформляется под заказ
Main image
Печать
DIPEPTIDYL PEPTIDASE IV
Кат. №: D4943-1VL
Производитель: Sigma-Aldrich
Кол-во:
Фасовка:
Цена по запросу
Товар оформляется под заказ
Description_x000D_ General description_x000D_ C-terminal histidine-tagged. Soluble form (residues 29-766) MW 105 kDa_x000D_ Application_x000D_ 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._x000D_ 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._x000D_ Biochem/physiol Actions_x000D_ 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._x000D_ 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._x000D_ Unit Definition_x000D_ 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._x000D_ Physical form_x000D_ Supplied as a solution in 10 mM Tris-HCl, pH 7.6, 200 mM NaCl, 1 mM EDTA and 10% glycerol._x000D_ Other Notes_x000D_ View more information on Dipeptidyl Peptidase IV at www.sigma-aldrich.com/enzymeexplorer.
Related Categories
3.4.x.x Peptidases, 3.x.x.x Hydrolases, Biochemicals and Reagents, Dipeptidyl peptidase IV, Enzyme Class Index, Enzymes, Inhibitors, and Substrates, Proteolytic Enzymes and Substrates, Selective Proteolytic EnzymesMore... Quality Level
Дорогой клиент, на сайте внедрена нейросеть для сбора информации о товаре. Это может привести к незначительным расхождениям в характеристиках продукции.
Description_x000D_ General description_x000D_ C-terminal histidine-tagged. Soluble form (residues 29-766) MW 105 kDa_x000D_ Application_x000D_ 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._x000D_ 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._x000D_ Biochem/physiol Actions_x000D_ 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._x000D_ 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._x000D_ Unit Definition_x000D_ 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._x000D_ Physical form_x000D_ Supplied as a solution in 10 mM Tris-HCl, pH 7.6, 200 mM NaCl, 1 mM EDTA and 10% glycerol._x000D_ Other Notes_x000D_ View more information on Dipeptidyl Peptidase IV at www.sigma-aldrich.com/enzymeexplorer.
Related Categories
3.4.x.x Peptidases, 3.x.x.x Hydrolases, Biochemicals and Reagents, Dipeptidyl peptidase IV, Enzyme Class Index, Enzymes, Inhibitors, and Substrates, Proteolytic Enzymes and Substrates, Selective Proteolytic EnzymesMore... Quality Level
Дорогой клиент, на сайте внедрена нейросеть для сбора информации о товаре. Это может привести к незначительным расхождениям в характеристиках продукции.