重组
expressed in E. coli
质量水平
方案
≥90% (SDS-PAGE)
表单
solution
比活
≥10 unit/μg protein
分子量
81.6 kDa
运输
dry ice
储存温度
−70°C
一般描述
Prolyl oligopeptidase (PO) is mapped to human chromosome 6q22. It comprises of a N-terminal β-propeller domain and C-terminal α/β hydrolase catalytic domain. PO is highly expressed in the neuronal cytoplasm and its expression increases with age.
Prolyl oligopeptidase is a cytosolic serine peptidase which cleaves peptide bonds at the C′ terminal side of prolines. It is only capable of processing peptides containing no more than 30 amino acids due to the unique β-propeller region that regulates access to the active site.
应用
Prolyl oligopeptidase has been used in a study to assess the mechanism of lithium ion action. It has also been used in a study to investigate its distribution in human tissue and body fluids.
Prolyl oligopeptidase has been used in the prolyl oligopeptidase inhibitory activity assay in lyophilized protein hydrolysate samples and Schistosoma mansoni samples.
生化/生理作用
Prolyl oligopeptidase (PO) regulates physiological processes and is crucial for the generation of active hormone and peptide fragments from their precursors. It shows elevated levels in psychiatric disorders and Alzheimer′s patients. Altered levels of PO is observed in patients with bipolar disorder. High expression of PO may promote metastasis of malignant ovarian and colorectal tumors.
外形
Supplied as a solution in 45 mM Tris-HCl, pH 8.0, 124 mM NaCl, 2.4 mM KCl, 10% glycerol, 3 mM DTT and variable amounts of imidazole.
制备说明
N-terminal GST-tagged 81.6 kDa full-length protein
其他说明
One unit will hydrolyze 1.0 picomole of Ala-Pro-aminomethylcoumarin per minute at pH 7.4 at 25 °C.
储存分类代码
12 - Non Combustible Liquids
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
常规特殊物品
此项目有
Mechanism of Action of Prolyl Oligopeptidase (PREP) in Degenerative Brain Diseases: Has Peptidase Activity Only a Modulatory Role on the Interactions of PREP with Proteins?
Mannisto PT, et al.
Frontiers in Aging Neuroscience, 9(3), 27-27 (2017)
Structure-function properties of prolyl oligopeptidase family enzymes
Rea D and Fulop V
Cell Biochemistry and Biophysics, 44(3), 349-365 (2006)
R S Williams et al.
The EMBO journal, 18(10), 2734-2745 (1999-05-18)
The therapeutic properties of lithium ions (Li+) are well known; however, the mechanism of their action remains unclear. To investigate this problem, we have isolated Li+-resistant mutants from Dictyostelium. Here, we describe the analysis of one of these mutants. This
Distribution of prolyl oligopeptidase in human peripheral tissues and in ovarian and colorectal tumors
Myohanen TT, et al.
The Journal of Histochemistry and Cytochemistry, 60(9), 706-715 (2012)
Prolyl oligopeptidase from the blood fluke Schistosoma mansoni: from functional analysis to anti-schistosomal inhibitors
Fajtova P, et al.
PLoS Neglected Tropical Diseases, 9(6), e0003827-e0003827 (2015)
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