焦谷氨酸氨肽酶 来源于激烈热球菌

P755320-0.01unit

0.01unit

重组

≥90%(SDS-PAGE)

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。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。应用： 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。 Pyroglutamate Aminopeptidase from Pyrococcus furiosus , also called the deblocking aminopeptidase, is a 42 kDa protein and belongs to aminopeptidase A family. It shares sequence homology with aminopeptidase in the active site, with conserved zinc and cobalt binding residues. Application: Pyroglutamate Aminopeptidase, from Pyrococcus furiosus is a recombinant, thermostable aminopeptidase that is expressed in Escherichia coli . It is used to cleave pyroglutamic acid which allows analysis of N-terminal sequences of peptides. The enzyme from Sigma has been used for the removal of pyroglutamate (pGlu) N-terminal blocking group, under reduced conditions, prior to N-terminal sequencing of purified cassiicolin. Thermostable aminopeptidase that liberates N-terminal pyroglutamic acid from proteins and peptides prior to Edman degradation.

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。