Analytical Data
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Gene name
GLO1/Glyoxalase I
- Application
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Alternative Names
Aldoketomutase Glyoxalase I
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Species
Human
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Source
E. coli
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Tag
N- GST
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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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Molecular Weight
47.8 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 an essential enzyme involved in the detoxification of methylglyoxal, a reactive dicarbonyl compound that can result from glycolysis and other metabolic processes. Elevated levels of methylglyoxal are linked to various pathophysiological conditions, including diabetes, neurodegenerative diseases, and cancer. As such, GLO1 plays a critical role in cellular defense against glycation and oxidative stress, thereby maintaining cellular homeostasis. The interest in GLO1 has surged, prompting researchers to focus on the recombinant production of this enzyme for both functional studies and therapeutic applications. By utilizing recombinant DNA technology, scientists can express GLO1 in suitable host systems, such as bacteria or yeast, allowing for the generation of large quantities of pure protein. This enables detailed biochemical characterization, kinetic studies, and investigation into the enzyme's mechanisms and regulation. Moreover, recombinant GLO1 can be used to explore its potential as a therapeutic target or biomarker in diseases associated with elevated methylglyoxal levels. Overall, the study of recombinant GLO1 not only enhances our understanding of its biological function but also opens avenues for novel strategies in treating glycation-related disorders.
