EGLP/GPX5 Protein, Pig (P.pastoris, Myc, His)

EGLP/GPX5 may constitute a protective system similar to glutathione peroxidase, protecting sperm membrane lipids from peroxidative damage. Despite the limited enzyme activity, the protective effect suggests an effect beyond enzyme function. EGLP/GPX5 Protein, Pig (P.pastoris, Myc, His) is the recombinant pig-derived EGLP/GPX5 protein, expressed by P. pastoris , with N-His, C-Myc labeled tag. The total length of EGLP/GPX5 Protein, Pig (P.pastoris, Myc, His) is 198 a.a., with molecular weight of ~26.1 kDa.

The EGLP/GPX5 protein emerges as a potential constituent of a protective system akin to glutathione peroxidase, safeguarding sperm membrane lipids against peroxide damage. Despite the limited enzymatic activity towards hydrogen peroxide or organic hydroperoxides exhibited by the purified porcine enzyme, the protective effect suggests a role beyond enzymatic function. Instead, EGLP/GPX5 may protect sperm from premature acrosome reaction in the epididymis by binding to lipid peroxides. This binding action could prevent the interaction of lipid peroxides with phospholipase A2, thereby mitigating the induction of the acrosome reaction. The multifaceted nature of EGLP/GPX5 implies its involvement in non-enzymatic mechanisms that contribute to the defense against peroxide-induced damage, highlighting its potential significance in preserving sperm viability and functionality. Further investigation is essential to unravel the specific molecular pathways and interactions orchestrated by EGLP/GPX5 in this protective capacity.

Pig

P. pastoris

N-His;C-Myc

O18994 (22N-219E)

396920  [NCBI]

NSNLEKMDCYKDVTGTIYDYDAFTLNGNEHIQFKQYAGKHVLFVNVATYCGLTAQYPELNTLQEELKPFGLVVLGFPCNQFGKQEPGENSEILLGLKYVRPGGGYVPNFQLFEKGDVNGEKEQKVFTFLKHSCPHPSELIGSIGYISWEPIRVHDIRWNFEKFLVGPDGVPVMRWVHETPISTVKSDILAYLKQFKTE

Approximately 26.1 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.