Analytical Data
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Gene name
frxA
- Application
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Alternative Names
frxA; Protein FrxA
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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
Q51795
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Expression Region
M1-E137
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Protein Length
Full Length
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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
FrxA (ferritin-like protein A) is a key protein involved in iron metabolism and homeostasis in various organisms. Its study is crucial due to the role of iron in essential biological processes, including oxygen transport, DNA synthesis, and electron transport. Dysregulation of iron homeostasis can lead to several health issues, such as anemia, neurodegenerative diseases, and other metabolic disorders. In recent years, researchers have focused on the recombinant expression of FrxA to better understand its structure and function. By producing FrxA as a recombinant protein in host systems like E. coli or yeast, scientists can obtain large quantities of the protein for biochemical assays, structural studies, and functional analyses. These studies aim to elucidate FrxA's mechanisms of iron binding and release, as well as its interactions with other cellular components. Additionally, understanding FrxA's role may contribute to the development of therapeutic strategies for iron-related diseases. As the demand for efficient iron metabolism becomes increasingly important in various biomedical contexts, the research on FrxA recombinant protein represents a significant advancement in the field of molecular biology and medical research.
