GLO1 Antibody (Rabbit mAb) [D11D19]

Application: Reactivity: Human, Mouse, Rat

Usage Information

Dilution
WB1:1000 IHC1:2000 IF1:50

Application
WB, IHC, IF

Reactivity
Human, Mouse, Rat

Source
Rabbit Monoclonal Antibody

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 Observed MW
21 kDa 36 kDa, 49 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Positive Control	Human colon carcinoma tissue; Human cerebrum tissue; Mouse liver cancer tissue; Human cerebellum tissue; Human colon tissue; Mouse cerebrum tissue; Human testis tissue; Human lung tissue; Rat testis tissue; Rat cerebellum tissue; Rat lung tissue; Mouse testis tissue; Mouse cerebral cortex tissue; Mouse lung tissue; HAP1 cells; C6 cells; L6 cells; C2C12 cells; PC-12 cells; MEF cells; HeLa cells; HepG2 cells
Negative Control

Positive Control

Human colon carcinoma tissue; Human cerebrum tissue; Mouse liver cancer tissue; Human cerebellum tissue; Human colon tissue; Mouse cerebrum tissue; Human testis tissue; Human lung tissue; Rat testis tissue; Rat cerebellum tissue; Rat lung tissue; Mouse testis tissue; Mouse cerebral cortex tissue; Mouse lung tissue; HAP1 cells; C6 cells; L6 cells; C2C12 cells; PC-12 cells; MEF cells; HeLa cells; HepG2 cells

Negative Control

Datasheet & SDS

Biological Description

Specificity
GLO1 Antibody (Rabbit mAb) [D11D19] detects endogenous levels of total GLO1 protein.

Clone
D11D19

Synonym(s)
Lactoylglutathione lyase, Aldoketomutase, Glyoxalase I, Ketone-aldehyde mutase, Methylglyoxalase, S-D-lactoylglutathione methylglyoxal lyase, Glx I, GLO1

Background
GLO1, glyoxalase I, is a homodimeric zinc-dependent metalloenzyme that catalyzes the first committed step of the glyoxalase detoxification system, converting the spontaneously formed hemithioacetal adduct of glutathione and methylglyoxal into S-D-lactoylglutathione. Methylglyoxal itself arises as an unavoidable, non-enzymatic byproduct of glycolysis, generated through trace-level degradation of the triose phosphate intermediates glyceraldehyde-3-phosphate and dihydroxyacetone phosphate, and this highly reactive dicarbonyl compound modifies both proteins and DNA to form advanced glycation end-products, including arginine-derived and deoxyguanosine-derived adducts, unless intercepted by GLO1. Because free glutathione reacts spontaneously and non-enzymatically with methylglyoxal to form the hemithioacetal substrate, GLO1's catalytic role begins downstream of this initial conjugation step, isomerizing the hemithioacetal through an enediolate intermediate mechanism rather than through hydride transfer, and the resulting S-D-lactoylglutathione is subsequently hydrolyzed by the downstream enzyme glyoxalase II to release D-lactate and regenerate free glutathione, completing the two-step detoxification cycle without net consumption of the glutathione cofactor. GLO1 activity is directly regulated by phosphorylation at threonine 107, catalyzed by calcium/calmodulin-dependent protein kinase II delta, and this phosphorylation event modulates GLO1's detoxification efficiency and proteomic integrity, providing a defined post-translational mechanism through which cellular calcium signaling tunes the rate of methylglyoxal clearance according to acute cellular stimuli rather than relying solely on changes in GLO1 protein abundance. Because GLO1 suppresses steady-state methylglyoxal concentration and thereby limits accumulation of methylglyoxal-derived protein and DNA adducts, GLO1 overexpression in tumor cells decreases sensitivity to a broad range of antitumor drugs, including alkylating agents, topoisomerase inhibitors, antitubulins, and antimetabolites, since these chemotherapeutic agents produce off-target increases in glycolytic flux and methylglyoxal generation that GLO1 activity counteracts; this effect is potentiated under hypoxic conditions, and elevated methylglyoxal levels activate the intrinsic apoptotic pathway partly through direct modification of spliceosomal proteins.

Background

GLO1, glyoxalase I, is a homodimeric zinc-dependent metalloenzyme that catalyzes the first committed step of the glyoxalase detoxification system, converting the spontaneously formed hemithioacetal adduct of glutathione and methylglyoxal into S-D-lactoylglutathione. Methylglyoxal itself arises as an unavoidable, non-enzymatic byproduct of glycolysis, generated through trace-level degradation of the triose phosphate intermediates glyceraldehyde-3-phosphate and dihydroxyacetone phosphate, and this highly reactive dicarbonyl compound modifies both proteins and DNA to form advanced glycation end-products, including arginine-derived and deoxyguanosine-derived adducts, unless intercepted by GLO1. Because free glutathione reacts spontaneously and non-enzymatically with methylglyoxal to form the hemithioacetal substrate, GLO1's catalytic role begins downstream of this initial conjugation step, isomerizing the hemithioacetal through an enediolate intermediate mechanism rather than through hydride transfer, and the resulting S-D-lactoylglutathione is subsequently hydrolyzed by the downstream enzyme glyoxalase II to release D-lactate and regenerate free glutathione, completing the two-step detoxification cycle without net consumption of the glutathione cofactor. GLO1 activity is directly regulated by phosphorylation at threonine 107, catalyzed by calcium/calmodulin-dependent protein kinase II delta, and this phosphorylation event modulates GLO1's detoxification efficiency and proteomic integrity, providing a defined post-translational mechanism through which cellular calcium signaling tunes the rate of methylglyoxal clearance according to acute cellular stimuli rather than relying solely on changes in GLO1 protein abundance. Because GLO1 suppresses steady-state methylglyoxal concentration and thereby limits accumulation of methylglyoxal-derived protein and DNA adducts, GLO1 overexpression in tumor cells decreases sensitivity to a broad range of antitumor drugs, including alkylating agents, topoisomerase inhibitors, antitubulins, and antimetabolites, since these chemotherapeutic agents produce off-target increases in glycolytic flux and methylglyoxal generation that GLO1 activity counteracts; this effect is potentiated under hypoxic conditions, and elevated methylglyoxal levels activate the intrinsic apoptotic pathway partly through direct modification of spliceosomal proteins.

References
https://pubmed.ncbi.nlm.nih.gov/34790575/ https://pubmed.ncbi.nlm.nih.gov/32966793/

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

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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%