D7052
Dipeptidyl Peptidase IV 来源于猪肾脏
lyophilized powder, ≥10 units/mg protein (Bradford)
别名:
Dipeptidyl aminopeptidase IV
表单
lyophilized powder
比活
≥10 units/mg protein (Bradford)
分子量
124 kDa
包装
vial of ≥0.75 unit
溶解性
0.1 M Tris-HCl, pH 8.0: soluble 1 vial/mL, clear, colorless
UniProt登记号
储存温度
−20°C
基因信息
pig ... DPPIV(397492)
应用
Dipeptidyl peptidase IV from porcine kidney has been used in a study to investigate engraftment of donor cells following hepatocyte transplantation. Dipeptidyl peptidase IV from porcine kidney has also been used in a study to investigate the metabolism of glucagon-like peptide-2.
The enzyme from sigma has been used in the determination of DPP-IV inhibitory activity of peptides in porcine skin gelatin hydrolysates.
生化/生理作用
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.
The pH optimum for the protease is 7.8-8.0. Dipeptidyl peptidase does not require activators. It is inhibited by diisopropyl fluorophosphate, phenylmethanesulfonyl fluoride, and diethyl p-nitrophenyl phosphate.
外形
Lyophilized powder containing Tris buffer salts
其他说明
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 8.0 at 37 °C.
警示用语：
Danger
危险分类
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
靶器官
Respiratory system
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
dust mask type N95 (US), Eyeshields, Gloves
法规信息
新产品
A J Kenny et al.
The Biochemical journal, 157(1), 169-182 (1976-07-01)
Dipeptidyl peptidase IV, an enzyme that releases dipeptides from substrates with N-terminal sequences of the forms X-Pro-Y or X-Ala-Y, was purified 300-fold from pig kidney cortex. The kidney is the main source of the enzyme, where it is one of
Dipeptidyl Peptidase-IV Inhibitory Activity of Peptides in Porcine Skin Gelatin Hydrolysates.
Hsu, Kuo-Chiang, et al.
Bioactive Food Peptides in Health and Disease, 205-205 (2013)
Kosho Yamanouchi et al.
Hepatology (Baltimore, Md.), 49(1), 258-267 (2008-11-13)
Engraftment of donor hepatocytes is a critical step that determines the success of hepatocyte transplantation. Rapid and efficient integration of donor cells would enable prompt liver repopulation of these cells in response to selective proliferative stimuli offered by a preparative
K M Fukasawa et al.
Biochimica et biophysica acta, 657(1), 179-189 (1981-01-15)
Dipeptidyl peptidase IV (dipeptidylpeptide hydrolase, EC 3.4.14.-) has been purified from the microsomal fraction of pig liver, using an immunoaffinity chromatography, and its properties compared with those of the enzyme purified from pig kidney. The amino acid compositions of both
Maegan L Capitano et al.
The Journal of clinical investigation, 129(6), 2555-2570 (2019-05-21)
The nuclear protein DEK is an endogenous DNA-binding chromatin factor regulating hematopoiesis. DEK is one of only 2 known secreted nuclear chromatin factors, but whether and how extracellular DEK regulates hematopoiesis is not known. We demonstrated that extracellular DEK greatly
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