Glutathione-S-Transferase (GST) Products

FYN proto-oncogene is a member of the Src family of tyrosine kinases, and has a molecular weight of 59kDa. Post-synthesis this protein is N-myristoylated on cytoplasmic polysomes.

Recombinant, rat GGTase I composed of an &#945- and a &#946-subunit (74 and 43 kDa, respectively). The &#945-subunit is expressed as a GST-fusion construct with an N-terminal His&#8226Tag sequence.

Glutathione disulfide (GSSG) is the oxidised dimeric form of glutathione (GSH), which is a naturally occuring tripeptide that takes part in the bodies detoxification mechanisms and protects against oxidative damage. Glutathione Oxidized acts as

Glutathione disulfide (GSSG) is the oxidised dimeric form of glutathione (GSH), which is a naturally occuring tripeptide that takes part in the bodies detoxification mechanisms and protects against oxidative damage. Glutathione Oxidized acts as

Glutathione peroxidase&nbspis an antioxidant enzyme that contains selenium. It is present in the glandular epithelium of human&nbspendometrium.

Glutathione peroxidase&nbspis an antioxidant enzyme that contains selenium. It is present in the glandular epithelium of human&nbspendometrium.

Glutathione peroxidase&nbspis an antioxidant enzyme that contains selenium. It is present in the glandular epithelium of human&nbspendometrium.

Glutathione is the major low molecular weight thiol compound of the living plant or animal cell. It is a tripeptide with a gamma peptide linkage between the amine group of cysteine (which is attached by normal peptide linkage to a glycine) and the

Glutathione suppresses human immunodeficiency virus expression in chronically infected monocytic cells. It is a useful tripeptide involved in many aspects of metabolism, including transport of g-glutanyl amino acids and reductive cleavage of

Glutathione S-transferase (GST) is a major detoxification enzyme, and exists as multiple cytoplasmic and membrane-bound isozymes. These isozymes differ in their catalytic activity, as well as in their non-catalytic binding properties.

Glutathione S-transferase (GST) is a major detoxification enzyme, and exists as multiple cytoplasmic and membrane-bound isozymes. These isozymes differ in their catalytic activity, as well as in their non-catalytic binding properties.

Glutathione S-transferase (GST) is a major detoxification enzyme, and exists as multiple cytoplasmic and membrane-bound isozymes. These isozymes differ in their catalytic activity, as well as in their non-catalytic binding properties.