Analytical Data
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Gene name
NR5A1
- Application
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Alternative Names
AD4BP; FTZF1; SF1
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Species
Human
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Source
E. coli
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Tag
Strep;His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q13285
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Expression Region
S218-T461, C247S, C412S
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Protein Length
Partial
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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
NR5A1, also known as steroidogenic factor 1 (SF-1), is a crucial transcription factor that plays a significant role in the regulation of various physiological processes, particularly those related to steroidogenesis, reproductive development, and metabolic homeostasis. Mutations in the NR5A1 gene can lead to a range of disorders, including adrenal insufficiency and disorders of sexual development, thereby highlighting its importance in human biology. The recombinant expression of NR5A1 protein has emerged as a critical tool for understanding its functional role in cellular signaling pathways. Researchers utilize recombinant NR5A1 to investigate its DNA-binding capabilities, interaction with other nuclear receptors, and its influence on target gene expression. By producing NR5A1 as a recombinant protein, scientists can study its structure-function relationships, elucidate mechanisms of its action in steroid hormone biosynthesis, and explore its potential implications in pathophysiological conditions. This research not only contributes to our understanding of endocrine function but also has potential applications in developing therapeutic strategies for diseases associated with NR5A1 dysfunction.
