Analytical Data
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Gene name
ER alpha/ESR1
- Application
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Alternative Names
ER-A1; ER; ESR; ESR1; ESRA; NR3A1; NR3-A1; Estrogen Receptor 1; Nuclear Receptor Subfamily 3,Group A,Member 1
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Species
Rat
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P06211
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Expression Region
Arg248~Leu484
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Molecular Weight
57kDa
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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
Estrogen receptor alpha (ER alpha), encoded by the ESR1 gene, is a crucial member of the nuclear receptor superfamily and plays a significant role in mediating the effects of estrogens in various physiological processes, including reproductive regulation, breast development, and bone maintenance. Abnormal ESR1 signaling has been implicated in numerous diseases, notably hormone-dependent cancers such as breast cancer. Studying the recombinant form of ER alpha allows researchers to explore its structure, function, and interactions with ligands and other proteins. This understanding is vital for developing targeted therapies that can modulate ER alpha activity. Additionally, the production of recombinant ER alpha facilitates high-throughput screening of potential drug compounds, thus accelerating drug discovery efforts in hormone-related disorders. Advances in protein expression systems have enabled the efficient generation of functional ER alpha, providing valuable insights into its ligand-binding domain, transcriptional activity, and post-translational modifications. As research continues to elucidate the complexities of ER alpha signaling pathways and their implications in health and disease, recombinant ER alpha remains a powerful tool for biotechnological and pharmaceutical advancements.
