Analytical Data
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Gene name
ELAVL1
- Application
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Alternative Names
ELAV-like protein 1; Hu-antigen R; HuR
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Species
Human
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Source
E. coli
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Tag
C-Flag
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q15717-1
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Expression Region
S2-K326
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Protein Length
Full Length of Isoform-1 Mature Protein
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Molecular Weight
35 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
ELAVL1, also known as HuR, is an RNA-binding protein that plays a crucial role in post-transcriptional regulation of gene expression. Its primary function involves stabilizing mRNA transcripts, thereby influencing the expression levels of various genes associated with cell proliferation, differentiation, and stress responses. Given its significant role in regulating mRNA stability and translation, ELAVL1 has been implicated in several pathological conditions, including cancer, neurodegenerative diseases, and inflammatory disorders. Research has demonstrated that elevated levels of ELAVL1 are often associated with tumor progression and increased cell survival, making it a potential therapeutic target. The study of ELAVL1 recombinant proteins allows researchers to dissect its functions, elucidate its binding mechanisms with RNA, and explore its interactions with other cellular factors. By generating and characterizing recombinant ELAVL1, scientists aim to understand how post-transcriptional regulation contributes to cell fate decisions and how dysregulation of this protein can lead to disease. Insights gained from such studies could pave the way for the development of novel therapeutic strategies targeting ELAVL1 in various biomedical contexts.
