Analytical Data
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Gene name
ERRa
- Application
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Alternative Names
ERRa；MAL；T-cell surface glycoProtein CD8 alpha chain
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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
231-330aa
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AA Sequence
LFDREIVVTISWAKSIPGFSSLSLSDQMSVLQSVWMEVLVLGVAQRSLPL QDELAFAEDLVLDEEGARAAGLGELGAALLQLVRRLQALRLEREEYVLLK
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Molecular Weight
37 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
ERRa (Estrogen-Related Receptor Alpha) is a member of the nuclear receptor superfamily, playing a crucial role in regulating gene expression related to metabolism, development, and reproduction. Initially identified for its structural similarity to estrogen receptors, ERRa is activated by endogenous ligands such as the metabolic byproducts of fat and is non-classically involved in signaling pathways that influence cellular energy homeostasis and adipogenesis. Research on ERRa has gained momentum due to its implication in various physiological processes and potential involvement in metabolic disorders, including obesity and type 2 diabetes, as well as certain cancers such as breast cancer. The study of ERRa and its recombinant protein forms has become pivotal in understanding its mechanism of action, ligand activation, and potential as a therapeutic target. Recent advancements in protein engineering techniques have enabled researchers to produce ERRa recombinant proteins, facilitating detailed Structural and functional studies, including crystallography and biochemical assays. These investigations aim to elucidate the role of ERRa in metabolic regulation and its interaction with other signaling pathways, enhancing our understanding of its therapeutic potential in metabolic diseases and cancer. Ultimately, the ongoing exploration of ERRa and its recombinant versions holds promise for developing novel strategies in disease prevention and treatment.
