P6236
焦谷氨酸氨肽酶 来源于激烈热球菌
recombinant, expressed in E. coli, ~90% (SDS-PAGE), ≥5.0 units/mg protein
别名:
L-吡咯烷酮羧基肽酶
产品名称
焦谷氨酸氨肽酶 来源于激烈热球菌, recombinant, expressed in E. coli, ~90% (SDS-PAGE), ≥5.0 units/mg protein
recombinant
expressed in E. coli
assay
~90% (SDS-PAGE)
form
lyophilized powder
specific activity
≥5.0 units/mg protein
mol wt
24.072 kDa by amino acid sequence
28 kDa by SDS-PAGE
shipped in
dry ice
storage temp.
−20°C
Quality Level
Application
在Edman降解之前，从蛋白质和肽中释放N-末端焦谷氨酸的热稳定氨肽酶。
在纯化的cassiicolin的N-末端测序之前，来自Sigma的酶已被用于在还原条件下除去焦谷氨酸（pGlu）N-末端封闭基团。
来自 强烈火球菌的焦谷氨酸氨基酞酶是一种重组的、热稳定的氨肽酶，其表达于 大肠杆菌。它可用于切割焦谷氨酸，从而对肽的N-末端序列进行分析。
Biochem/physiol Actions
焦谷氨酸氨肽酶（PGP 1）可与免疫球蛋白发生相互作用，起炎性细胞因子的作用并调节免疫应答。 PGP 1水平在炎症期间升高。
该酶对N-末端焦谷氨酸具有特异性。它在Edman降解之前，可从蛋白质和肽中切割N-末端焦谷氨酸。其最适温度范围为95至100°C，最适pH范围为6.0至9.0。
General description
来自 强烈火球菌的焦谷氨酸氨基酞酶也被称为解封闭氨肽酶，是一种42kDa的蛋白质，属于氨肽酶A家族。它与活性位点中的氨肽酶具有序列同源性，具有保守的锌和钴结合残基。
Other Notes
在pH 7.0，37 °C条件下，一个单位每分钟可水解1 μmol焦谷氨酸对硝基苯胺。
Physical form
含有磷酸钠的冻干粉
Preparation Note
用含有10mM DTT和1mM EDTA的50 μl 50mM磷酸钠（pH 7.0）溶液重溶瓶中的酶。重溶的溶液应储存在-20°C。
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
常规特殊物品
此项目有
Frédéric de Lamotte et al.
Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 849(1-2), 357-362 (2006-11-23)
Cassiicolin, a phytotoxin produced by the necrotrophic fungus Corynespora cassiicola, was purified to homogeneity from a rubber tree isolate. The optimized protocol involves reverse phase chromatography followed by size exclusion chromatography, with monitoring of the toxicity on detached rubber tree
New deblocking aminopeptidases from Pyrococcus horikoshii
Mori K and Ishikawa K
Bioscience, Biotechnology, and Biochemistry, 69(10), 1854-1860 (2005)
Pyroglutamate aminopeptidase 1 may be an indicator of cellular inflammatory response as revealed using a sensitive long-wavelength fluorescent probe
Gong Q, et al.
Chemical Science, 7(7), 4694-4697 (2016)
A Ultrasensitive Near-Infrared Fluorescent Probe Reveals Pyroglutamate Aminopeptidase 1 Can Be a New Inflammatory Cytokine
Gong Q, et al.
Advanced science (Weinheim, Baden-Wurttemberg, Germany), 5(4), 1700664-1700664 (2018)
Johanna L Hellström et al.
Biochimica et biophysica acta, 1764(11), 1735-1740 (2006-10-20)
To enable Edman sequencing of pyroglutamylated immunoglobulins, enzymatic deblocking by pyroglutamate aminopeptidase is performed, often with variable yield and compromised solubility. Recently, enzymatic deblocking of immunoglobulins without denaturation was described. Although the conditions ensured efficient removal of pyroglutamyl residues, we
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