Analytical Data
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Gene name
RARa
- Application
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Alternative Names
RARa；NR1B1；Retinoic acid receptor 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
P10276
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Expression Region
1-462aa
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AA Sequence
MASNSSSCPT PGGGHLNGYP VPPYAFFFPP MLGGLSPPGA LTTLQHQLPV SGYSTPSPAT IETQSSSSEE IVPSPPSPPP LPRIYKPCFV CQDKSSGYHY GVSACEGCKG FFRRSIQKNM VYTCHRDKNC IINKVTRNRC QYCRLQKCFE VGMSKESVRN DRNKKKKEVP KPECSESYTL TPEVGELIEK VRKAHQETFP ALCQLGKYTT NNSSEQRVSL DIDLWDKFSE LSTKCIIKTV EFAKQLPGFT TLTIADQITL LKAACLDILI LRICTRYTPE QDTMTFSDGL TLNRTQMHNA GFGPLTDLVF AFANQLLPLE MDDAETGLLS AICLICGDRQ DLEQPDRVDM LQEPLLEALK VYVRKRRPSR PHMFPKMLMK ITDLRSISAK GAERVITLKM EIPGSMPPLI QEMLENSEGL DTLSGQPGGG GRDGGGLAPP PGSCSPSLSP SSNRSSPATH SP
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Molecular Weight
50.7 kDa
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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
RARa (Retinoic Acid Receptor Alpha) is a nuclear receptor that plays a crucial role in mediating the effects of retinoic acid, a derivative of vitamin A, on gene expression and cellular differentiation. Research on RARa has gained significant attention due to its involvement in various biological processes, including embryonic development, immunity, and metabolism. Moreover, RARa is a critical player in the development of certain malignancies, particularly in acute promyelocytic leukemia (APL), where its fusion with the promyelocytic leukemia (PML) gene results in the disruption of normal differentiation and proliferation pathways. The study of RARa recombinant proteins has become an essential tool for understanding its functional mechanisms, interaction with endogenous ligands, and its role in gene regulation. By producing RARa as a recombinant protein, researchers can elucidate the structure-function relationships, identify potential binding partners, and screen for small molecules that modulate its activity. This research is not only vital for advancing our understanding of RARa's role in normal physiology but also has potential therapeutic implications in diseases where RARa is implicated, including cancer and other disorders related to retinoic acid signaling. Overall, the investigation of RARa recombinant proteins represents an important frontier in molecular biology, drug discovery, and the development of targeted therapies.
