Analytical Data
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Gene name
ESRRA
- Application
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Alternative Names
Estrogen receptor-like 1 Estrogen-related receptor alpha
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P11474
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Expression Region
1-423aa
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Molecular Weight
72.5 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 research on ESRRA (Estrogen Related Receptor Alpha) recombinant proteins is anchored in the significant role this nuclear receptor plays in various physiological processes, including metabolism, development, and cellular differentiation. Identified as a key modulator in the regulation of genes involved in energy homeostasis, ESRRA is increasingly recognized for its implications in metabolic disorders such as obesity and diabetes, as well as in certain types of cancer, particularly those influenced by hormonal signaling. The interest in recombinant ESRRA proteins has surged as researchers aim to elucidate their structure-function relationships and to explore their potential as therapeutic targets. This has been facilitated by advances in protein engineering and expression systems, allowing for the generation of functional recombinant proteins that can be used in biochemical assays and functional studies. Understanding the mechanistic pathways involving ESRRA is crucial for developing novel interventions that could modify its activity, thereby providing new avenues for treating metabolic diseases and hormone-related cancers. Moreover, the study of ESRRA recombinant proteins paves the way for innovative research into the intricate regulatory networks underlying gene expression in response to environmental changes and hormonal signals, shedding light on the multifaceted roles of this receptor in health and disease.
