Analytical Data
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Gene name
RXRA
- Application
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Alternative Names
RXRA;NR2B1;Retinoic acid receptor RXR-alpha
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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
P19793
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Expression Region
1-462aa
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AA Sequence
MDTKHFLPLD FSTQVNSSLT SPTGRGSMAA PSLHPSLGPG IGSPGQLHSP ISTLSSPING MGPPFSVISS PMGPHSMSVP TTPTLGFSTG SPQLSSPMNP VSSSEDIKPP LGLNGVLKVP AHPSGNMASF TKHICAICGD RSSGKHYGVY SCEGCKGFFK RTVRKDLTYT CRDNKDCLID KRQRNRCQYC RYQKCLAMGM KREAVQEERQ RGKDRNENEV ESTSSANEDM PVERILEAEL AVEPKTETYV EANMGLNPSS PNDPVTNICQ AADKQLFTLV EWAKRIPHFS ELPLDDQVIL LRAGWNELLI ASFSHRSIAV KDGILLATGL HVHRNSAHSA GVGAIFDRVL TELVSKMRDM QMDKTELGCL RAIVLFNPDS KGLSNPAEVE ALREKVYASL EAYCKHKYPE QPGRFAKLLL RLPALRSIGL KCLEHLFFFK LIGDTPIDTF LMEMLEAPHQ MT
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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
The RXRA (Retinoid X Receptor Alpha) protein is a member of the nuclear receptor superfamily that plays a critical role in mediating the biological effects of retinoic acid and other ligands involved in various physiological processes. RXRA functions as a heterodimer with other nuclear receptors, influencing gene expression related to lipid metabolism, cell differentiation, and signaling pathways. Research surrounding the recombination of RXRA focuses on its potential implications in metabolic disorders, cancer, and developmental abnormalities. The ability to manipulate RXRA through recombinant protein technology enables scientists to study its functional mechanisms and interactions in-depth, shedding light on its role in various diseases. Additionally, RXRA is a target for pharmacological interventions, making its characterization through recombinant methodologies vital for the development of novel therapies. Recent advancements in protein engineering and expression systems have enhanced the yield and functionality of RXRA-derived proteins, allowing for a more robust assessment of their biological activities. Understanding the intricate workings of RXRA and its reconstitution can lead to significant insights into therapeutic strategies for conditions affected by its dysfunction, highlighting the importance of continued research in this area.
