Datasheet

Biological Description

Specificity	Anti-GGT1/GGT Mouse Antibody [N21M12] detects endogenous levels of total GGT1/GGT protein.
Background	γ-Glutamyltranspeptidase (GGT) is a widely distributed enzyme that belongs to the superfamily of N-terminal nucleophilic hydrolases, characterized by an N-terminal catalytic residue responsible for cleaving amide bonds. Functionally, GGT catalyzes the breakdown of the γ-glutamyl amide bond from donor substrates and transfers the liberated γ-glutamyl group either to water, resulting in hydrolysis, or to amino acids and short peptides, resulting in transpeptidation. GGT is located on the external surface of cell membranes, where it plays a central role in glutathione (GSH) metabolism—the major intracellular antioxidant thiol. By hydrolyzing extracellular GSH, GGT facilitates the recovery of cysteine, an essential precursor for de novo synthesis of intracellular GSH and proteins. Through this mechanism, GGT contributes to redox balance and enhances cellular resistance to oxidative stress, thereby supporting rapid cell proliferation. Notably, GGT expression is elevated in inflammatory states and during the progression of several cancers. Its dysregulation has also been associated with a variety of oxidative stress–related pathologies, including cardiovascular disease and diabetes.

Specificity

Anti-GGT1/GGT Mouse Antibody [N21M12] detects endogenous levels of total GGT1/GGT protein.

Background

γ-Glutamyltranspeptidase (GGT) is a widely distributed enzyme that belongs to the superfamily of N-terminal nucleophilic hydrolases, characterized by an N-terminal catalytic residue responsible for cleaving amide bonds. Functionally, GGT catalyzes the breakdown of the γ-glutamyl amide bond from donor substrates and transfers the liberated γ-glutamyl group either to water, resulting in hydrolysis, or to amino acids and short peptides, resulting in transpeptidation. GGT is located on the external surface of cell membranes, where it plays a central role in glutathione (GSH) metabolism—the major intracellular antioxidant thiol. By hydrolyzing extracellular GSH, GGT facilitates the recovery of cysteine, an essential precursor for de novo synthesis of intracellular GSH and proteins. Through this mechanism, GGT contributes to redox balance and enhances cellular resistance to oxidative stress, thereby supporting rapid cell proliferation. Notably, GGT expression is elevated in inflammatory states and during the progression of several cancers. Its dysregulation has also been associated with a variety of oxidative stress–related pathologies, including cardiovascular disease and diabetes.

Usage Information

Application

WB, IHC, IF, FCM

Dilution

WB

1:1000

Reactivity

Mouse, Human

Source

Mouse

MW

61 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/37739139/

Anti-GGT1/GGT Mouse Antibody [N21M12]

Biological Description

Usage Information

References

Application Data