Analytical Data
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Gene name
RARg
- Application
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Alternative Names
NR1B3; RARC; Nuclear receptor subfamily 1 group B member 3
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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
P13631
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Expression Region
Asp178~Glu423
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Molecular Weight
23kDa
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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
RARγ (Retinoic Acid Receptor Gamma) is a member of the nuclear receptor superfamily that plays a crucial role in various biological processes, including development, immune function, and metabolism. Its activation by retinoic acid, a derivative of vitamin A, regulates gene expression involved in cell differentiation and proliferation. Dysregulation of RARγ has been implicated in several pathological conditions, including cancer and autoimmune diseases. Research into RARγ recombinant proteins has gained traction due to their potential therapeutic applications. Scientists have been exploring RARγ's structural and functional properties to understand its signaling pathways better and identify small molecules that can modulate its activity. The development of RARγ recombinant proteins allows for detailed studies of its interactions with ligands and co-regulators, contributing to a deeper understanding of its biological functions and the molecular mechanisms underlying related diseases. Furthermore, RARγ has emerged as a promising drug target, as compounds that can enhance or inhibit its activity could lead to novel treatments for conditions like acute promyelocytic leukemia (APL) and other disorders linked to retinoic acid signaling. Thus, the ongoing research on RARγ recombinant proteins is essential for unraveling its complex role in physiological and pathological contexts, paving the way for innovative therapeutic strategies.
