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Anti-GGT1/GGT Mouse Antibody [N21M12]

Catalog No.: F2746

Application: Reactivity: Mouse, Human

Usage Information

Dilution
WB1:1000

Application
WB, IHC, IF, FCM

Reactivity
Mouse, Human

Source
Mouse

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

Predicted MW
61 kDa

Datasheet & SDS

Biological Description

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

Clone
N21M12

Synonym(s)
CD224, GGT, GGT1, Glutathione hydrolase 1 proenzyme, Gamma-glutamyltransferase 1, Gamma-glutamyltranspeptidase 1, Leukotriene-C4 hydrolase, GGT 1

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.

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.

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

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

Tech Support

Answers to questions you may have can be found in the inhibitor handling instructions. Topics include how to prepare stock solutions, how to store inhibitors, and issues that need special attention for cell-based assays and animal experiments.

Handling Instructions

Tel: +1-832-582-8158 Ext:3
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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%