Analytical Data
-
Gene name
ERRa
- Application
-
Alternative Names
ERR1; ERRa; ERRalpha; ESRL1; NR3B1; Estrogen receptor-like 1; Nuclear receptor subfamily 3 group B member 1
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P11474
-
Expression Region
Pro193~Met421
-
Molecular Weight
33kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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 that plays a crucial role in various biological processes, including energy metabolism, cardiovascular physiology, and development. Initially identified as a transcription factor related to estrogen signaling, ERRa has garnered attention due to its involvement in the regulation of genes associated with mitochondrial function and oxidative metabolism. Furthermore, its dysregulation has been linked to several metabolic disorders, cancers, and cardiovascular diseases, making it a significant target for therapeutic intervention. Research into ERRa has expanded to explore its role in modulating metabolic pathways, cellular differentiation, and response to hormonal signals. The study of ERRa's recombinant protein has become pertinent to understanding its structure-function relationships, interaction with co-regulators, and its potential as a biomarker or drug target in various diseases. By producing ERRa as a recombinant protein, researchers aim to elucidate its mechanisms of action, enhance our understanding of its role in pathophysiology, and develop novel strategies for targeted therapies in conditions where ERRa signaling is altered.
