Analytical Data
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Gene name
frmA
- Application
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Alternative Names
(Alcohol dehydrogenase class-3)(Alcohol dehydrogenase class-III)(Glutathione-dependent formaldehyde dehydrogenase)(FALDH)(FDH)(GSH-FDH)
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q1RFI7
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Expression Region
1-369aa
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Molecular Weight
46.8 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
The study of frmA recombinant protein is situated at the intersection of microbiology and biotechnology, focusing on the frmA gene found in various microbial species. This gene encodes for the enzyme Formyltetrahydrofolate synthetase, which plays a crucial role in the folate biosynthesis pathway, essential for microbial growth and metabolism. Understanding frmA is particularly significant in the context of antibiotic resistance, as folate synthesis is a target for several antimicrobial agents. By exploring the structure and function of frmA recombinant protein, researchers aim to elucidate its mechanism of action and its potential application in developing new antibiotics or enhancing existing therapeutic strategies. Additionally, the expression and characterization of frmA can provide insights into microbial physiology and the adaptive responses of microorganisms to environmental changes. Given the global rise of multidrug-resistant pathogens, the ongoing research into frmA recombinant protein presents valuable opportunities for the discovery of novel biopharmaceuticals and contributes to the broader field of microbial genetics and metabolic engineering.
