GSTP1 Protein, Human (P.pastoris, His)

The GSTP1 protein is critical for binding reduced glutathione to a variety of hydrophobic electrophiles, actively forming glutathione conjugates of PGA2 and PGJ2. Documented studies highlight its involvement in hepoxilin regioisomer synthesis, emphasizing the versatility of GSTP1 in processing substrates. GSTP1 Protein, Human (P.pastoris, His) is the recombinant human-derived GSTP1 protein, expressed by P. pastoris , with N-His labeled tag. The total length of GSTP1 Protein, Human (P.pastoris, His) is 209 a.a., with molecular weight of ~25.7 kDa.

The GSTP1 protein plays a crucial role in the cellular process of conjugating reduced glutathione to a diverse range of exogenous and endogenous hydrophobic electrophiles. Specifically, GSTP1 is actively involved in the formation of glutathione conjugates for prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2), as documented in studies. Furthermore, GSTP1 participates in the synthesis of novel hepoxilin regioisomers, underscoring its versatility in handling various substrates. Beyond its role in detoxification, GSTP1 negatively regulates CDK5 activity by facilitating the translocation of p25/p35, serving as a crucial mechanism to prevent neurodegeneration.

Human

P. pastoris

N-His

P09211 (P2-Q210)

2950  [NCBI]

PPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLIHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNLPINGNGKQ

Approximately 25.7 kDa

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

<1 EU/μg, determined by LAL method.