Abcam, ab87413, Recombinant human GLO1 protein

Size: 100µg
Recombinant human GLO1 protein is a Human Full Length protein, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, FuncS.
Key facts
Purity:>90% SDS-PAGE,
Expression system:Escherichia coli,
Tags:Tag free,
Applications:FuncS, SDS-PAGESee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:Yes,
Biological activity:Specific activity: >0.4 units/mg (please enquire for specific batch value). One unit will form 1.0 μmol of S-lactoylglutathione from methylglyoxal and reduced glutathione per minute at pH 7.5, at 25°C. Specific activity was expressed in units/mg of protein.,
Accession:Q04760,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 8Constituents: 10% Glycerol (glycerin, glycerine), 0.316% Tris HCl, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

Product details:
Activity Assay
Final assay concentrations:
In 1.5ml reaction mix, the final concentrations are 79 mM potassium phosphate, 0.033%(w/v) reduced glutathine, 0.003% (w/v) bovine serum albumin, 0.033% methylglyoxal(w/v) and recombinant gyloxalase l (0.5ug, 1ug, 2ug).
1. Prepare protein-free reaction buffer without recombinant protein into suitable container (for each protein concentration).
2. Equilibrate protein-free reaction buffer to 25°C and monitor at A240nm (absorbance) until the value is constant, using a spectrophotometer.
3. Dilute various concentrations of recombinant gyloxalase l (0.5ug, 1ug, 2ug) in 50ul of 10mM potassium phosphate buffer with 0.1% (wv) BSA, pH7.4.
Add 50ul of recombinant glyoxalase I solution to 1.45ml reaction buffer.
Immediately mix by inversion and record the increase at A240nm for 5 minutes

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
The GLO1 protein also known as glyoxalase I plays an important role in cellular metabolism by detoxifying methylglyoxal a byproduct of glycolysis. It catalyzes the conversion of methylglyoxal into S-D-lactoylglutathione using glutathione as a cofactor. This enzyme has a mass of approximately 29 kDa and is expressed in various tissues throughout the body with higher levels found in the liver and kidney. Glyoxalase I (GLO1) expression is increased in response to stress conditions indicating its role in cellular defense mechanisms.
Biological function summary
Glyoxalase I is important for maintaining cellular homeostasis by mitigating harmful compounds. It forms part of the glyoxalase system which includes glyoxalase II functioning downstream of GLO1. This system prevents the accumulation of advanced glycation end-products (AGEs) which are implicated in cellular aging and dysfunction. By reducing the levels of methylglyoxal GLO1 supports normal physiological processes and protects cellular integrity.
Pathways
Glyoxalase I is an important component of the glyoxalase pathway. This pathway integrates into the detoxification network working alongside other important enzymes such as superoxide dismutase and catalase. These relationships highlight its function in cellular oxidative stress responses. GLO1's activity impacts pathways related to glycolysis and overall energy metabolism due to its role in reducing metabolic byproducts.
GLO1 has significant implications in diabetic complications and cancer. In diabetes increased methylglyoxal can worsen tissue damage making GLO1's role protective against advanced glycation end-product formation. In cancer GLO1 is overexpressed contributing to cellular proliferation and survival. Its interaction with proteins such as Hsp70 in cancer illustrates the adaptive mechanisms that tumor cells use for progression and chemoresistance.