Analytical Data
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Gene name
RXRg
- Application
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Alternative Names
NR2B3; RXRC; Nuclear receptor subfamily 2 group B member 3; Retinoic acid receptor RXR-gamma
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P48443
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Expression Region
Pro12~Ala220
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Molecular Weight
29kDa
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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
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Protein Description
RXRg, or Retinoid X Receptor gamma, is a member of the nuclear receptor superfamily that plays a crucial role in various biological processes, including metabolism, cell differentiation, and immune response. Its function is significantly influenced by its ability to form heterodimers with other nuclear receptors, which modulates gene expression in response to retinoids and fatty acids. Dysfunction or aberrant signaling of RXRg has been implicated in several pathological conditions, such as obesity, diabetes, and certain types of cancer. Research on RXRg has garnered interest due to its potential as a therapeutic target, particularly in the context of metabolic disorders and cancer, where modulation of its activity could yield beneficial effects. The recombinant expression of RXRg in various systems enables detailed structural and functional studies, facilitating the discovery of small molecules that can selectively modulate its activity. Recent advances in protein engineering and structural biology have provided insights into the ligand-binding domain and the conformational changes associated with RXRg activation. Understanding the precise mechanisms of RXRg action and its interactions at the molecular level is critical for the development of innovative therapeutic strategies aimed at harnessing its function for disease intervention. As such, RXRg serves as a pertinent focus of research within the fields of pharmacology and molecular biology, underscoring its relevance in understanding complex regulatory networks.











