Analytical Data
-
Gene name
ER beta/ESR2
- Application
-
Alternative Names
Nuclear receptor subfamily 3 group A member 2
-
Species
Human
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q92731
-
Expression Region
2-323aa
-
Molecular Weight
39.8 kDa
-
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
Estrogen receptors (ERs) are crucial members of the nuclear receptor superfamily, playing vital roles in mediating the effects of estrogen on various tissues. Among them, ER beta (ERβ), also known as estrogen receptor 2 (ESR2), has garnered significant attention due to its unique expression patterns and distinct physiological functions compared to its counterpart ER alpha (ERα). Research has demonstrated that ERβ is involved in diverse processes, including reproductive health, bone maintenance, and neuroprotection, making it a potential therapeutic target for a range of conditions, such as osteoporosis, breast cancer, and neurodegenerative disorders. Characterizing the structure and function of ERβ through recombinant protein technology is essential for understanding its signaling mechanisms and developing selective ERβ modulators. By producing recombinant ERβ proteins, researchers can elucidate the receptor's interactions with ligands and co-regulators, shedding light on its role in gene expression and cellular signaling pathways. This research is pivotal for advancing our knowledge of estrogen signaling, ultimately aiding in the design of targeted therapies that leverage the beneficial effects of ERβ while minimizing side effects associated with non-selective estrogenic compounds.
