Analytical Data
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Gene name
GLO1
- Application
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Alternative Names
GLO1;Lactoylglutathione lyase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q04760
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Expression Region
1-184aa
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AA Sequence
MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYT RVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLE LTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFV KKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM
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Molecular Weight
21 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Glyoxalase I (GLO1) is a key enzyme in the detoxification of methylglyoxal (MG), a reactive dicarbonyl compound generated as a byproduct of glycolysis. Elevated levels of MG are associated with various diseases, including diabetes, neurodegenerative disorders, and cancer, due to its ability to induce protein glycation and oxidative stress. GLO1 catalyzes the conversion of MG and reduced glutathione into S-D-lactoylglutathione, thereby protecting cells from MG-induced damage. The study of recombinant GLO1 has gained significant interest as it offers insights into the enzyme's structure-function relationship, catalytic mechanisms, and potential as a therapeutic target. Advances in molecular biology and protein expression systems have facilitated the production of recombinant GLO1, enabling detailed kinetic and biochemical analyses. Researchers aim to elucidate the role of GLO1 in human health and disease, explore its potential as a biomarker, and develop novel therapeutic strategies that enhance its activity or mimic its function to mitigate MG-related pathologies. Understanding the regulation of GLO1 and its interplay with other cellular pathways may pave the way for innovative treatments in conditions where MG accumulation is detrimental.
