Recombinant Human GSS Protein (His Tag) | PKSH032497

Recombinant Human GSS Protein (His Tag) | PKSH032497 | Gentaur US, UK & Europe Disrtribition

Synonyms: Glutathione Synthetase; GSH Synthetase; GSH-S; Glutathione Synthase; GSS

Active Protein: N/A

Activity: Recombinant Human Glutathione Synthetase is produced by our E.coli expression system and the target gene encoding Ala2-Val474 is expressed with a 6His tag at the C-terminus.

Protein Construction: Recombinant Human Glutathione Synthetase is produced by our E.coli expression system and the target gene encoding Ala2-Val474 is expressed with a 6His tag at the C-terminus.

Fusion Tag: C-6His

Species: Human

Expressed Host: E.coli

Shipping: This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs. Upon receipt, store it immediately at<-20°C.

Purity: > 95 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

Stability and Storage: Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles.

Molecular Mass: 53.5 kDa

Formulation: Supplied as a 0.2 μm filtered solution of 20mM TrisHCl, 200mM NaCl, pH 7.5 .

Reconstitution: Not Applicable

Background: Glutathione Synthetase belongs to the eukaryotic GSH synthase family. Glutathione Synthetase is the second enzyme in the glutathione biosynthesis pathway. It catalyses the condensation of gamma-glutamylcysteine and glycine to form glutathione. Glutathione play an important role in a variety of biological functions, including detoxification of xenobiotics, protection of cells from oxidative damage by free radicals, and membrane transport. The protein functions as a homodimer to catalyze the second step of glutathione biosynthesis, which is the ATP-dependent conversion of gamma-L-glutamyl-L-cysteine to glutathione. Defects in Glutathione Synthetase can also cause the glutathione synthetase deficiency of erythrocytes, which is a mild form causing hemolytic anemia.

Research Area: Signal Transduction, Cell biology, Neuroscience, metabolism,