Analytical Data
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Gene name
RBED1
- Application
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Alternative Names
ELMOD3; RBED1; RBM29; PP4068ELMO domain-containing protein 3; RNA-binding motif and ELMO domain-containing protein 1; RNA-binding motif protein 29; RNA-binding protein 29
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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
Q96FG2
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Expression Region
1-381 aa
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AA Sequence
MNEKSCSFHS KEELRDGQGE RLSAGYSPSY DKDKSVLAFR GIPISELKNH GILQALTTEA YEWEPRVVST EVVRAQEEWE AVDTIQPETG SQASSEQPGQ LISFSEALQH FQTVDLSPFK KRIQPTIRRT GLAALRHYLF GPPKLHQRLR EERDLVLTIA QCGLDSQDPV HGRVLQTIYK KLTGSKFDCA LHGNHWEDLG FQGANPATDL RGAGFLALLH LLYLVMDSKT LPMAQEIFRL SRHHIQQFPF CLMSVNITHI AIQALREECL SRECNRQQKV IPVVNSFYAA TFLHLAHVWR TQRKTISDSG FVLKELEVLA KKSPRRLLKT LELYLARVSK GQASLLGAQK CYGPEAPPFK DLTFTGESDL QSHSSEGVWL I
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Molecular Weight
43.0 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
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Protein Description
RBED1, a protein implicated in various biological processes, has gained attention in recent years due to its potential roles in gene regulation, cell proliferation, and apoptosis. Studies have shown that RBED1 can interact with key regulatory proteins, influencing pathways related to tumor suppression and cellular stress responses. Understanding the structure and function of RBED1 is crucial, as it may serve as a biomarker for certain diseases or a target for therapeutic interventions. Recent research efforts have focused on the recombinant expression of RBED1, allowing for the production of purified protein for in-depth functional assays and biochemical characterization. By utilizing techniques such as bacterial expression systems and purification through affinity chromatography, researchers aim to elucidate the mechanistic insights into RBED1's role at the molecular level. Preliminary findings suggest that modifications in RBED1 activity may have implications for cancer biology and other complex diseases, highlighting the necessity for continued investigation into this protein's function and its potential therapeutic applications.
