Analytical Data
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Gene name
GAL5
- Application
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Alternative Names
Lgals5; RL-18
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P47967
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Expression Region
Met1~Thr145
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Molecular Weight
18kDa
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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
GAL5 is a gene that encodes a protein involved in the galactose metabolism pathway in yeast. Research into GAL5 recombinant protein has gained significance due to its potential applications in biotechnology and industrial fermentation processes. The study of GAL5 is particularly relevant because of the increasing interest in using renewable resources for bioproduction. Galactose is a common sugar found in dairy products and various plant materials, and harnessing GAL5 can improve the utilization of these resources for the production of biofuels, biochemicals, and food additives. By understanding the structure and function of the GAL5 protein, scientists aim to elucidate its role in enzymatic reactions and metabolic regulation. Recombinant technology allows for the production of GAL5 in microbial systems, enabling researchers to study its properties in detail and potentially modify it for enhanced performance. Furthermore, the insights gained from GAL5 studies may contribute to the development of more efficient microbial strains that can thrive on galactose-rich substrates, facilitating a more sustainable approach to industrial processes. Overall, GAL5 represents a critical component in the ongoing exploration of metabolic engineering and synthetic biology, with the potential to drive advancements in various fields, including fermentation technology and bioinformatics.
