Analytical Data
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Gene name
Galactokinase
- Application
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Alternative Names
Galactokinase
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Species
Others
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q5SKP8
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Expression Region
M1-L347
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Protein Length
Full Length
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Molecular Weight
37.6 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
Galactokinase (GalK) is an essential enzyme that catalyzes the first step in the galactose metabolism pathway, converting galactose into galactose-1-phosphate (Gal-1-P) in the presence of ATP. Deficiency in galactokinase activity can lead to a rare genetic disorder known as galactosemia, which results in the accumulation of galactose and its metabolites, ultimately causing severe health issues such as cataracts, liver damage, and intellectual disabilities. The study of recombinant GalK has gained significant attention in recent years due to its potential implications in biotechnology and medicine. By expressing and purifying GalK through recombinant DNA technology, researchers can gain insights into its structure, function, and regulation. Understanding the enzyme's kinetics, substrate specificity, and interaction with other metabolic pathways is crucial for developing therapeutic strategies for galactosemia and other metabolic disorders. Additionally, recombinant GalK can be utilized in synthetic biology applications, such as the production of biofuels or biochemicals from galactose-rich substrates. The exploration of GalK’s properties through structural biology techniques, such as X-ray crystallography and nuclear magnetic resonance (NMR), may reveal critical details about its active site and mechanism of action, paving the way for enzyme engineering efforts aimed at enhancing its activity or stability. Overall, the comprehensive study of recombinant GalK provides valuable knowledge that could advance our understanding of carbohydrate metabolism and its relevance in health and disease.
