Analytical Data
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Gene name
CELF1
- Application
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Alternative Names
CELF1；BRUNOL2；CUGBP；CUGBP1；CUGBP Elav-like family member 1
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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
Q92879
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Expression Region
1-486aa
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AA Sequence
MNGTLDHPDQPDLDAIKMFVGQVPRTWSEKDLRELFEQYGAVYEINVLRDRSQNPPQSKGCCFVTFYTRKAALEAQNALHNMKVLPGMHHPIQMKPADSEKNNAVEDRKLFIGMISKKCTENDIRVMFSSFGQIEECRILRGPDGLSRGCAFVTFTTRAMAQTAIKAMHQAQTMEGCSSPMVVKFADTQKDKEQKRMAQQLQQQMQQISAASVWGNLAGLNTLGPQYLALYLQLLQQTASSGNLNTLSSLHPMGGLNAMQLQNLAALAAAASAAQNTPSGTNALTTSSSPLSVLTSSGSSPSSSSSNSVNPIASLGALQTLAGATAGLNVGSLAGMAALNGGLGSSGLSNGTGSTMEALTQAYSGIQQYAAAALPTLYNQNLLTQQSIGAAGSQKEGPEGANLFIYHLPQEFGDQDLLQMFMPFGNVVSAKVFIDKQTNLSKCFGFVSYDNPVSAQAAIQSMNGFQIGMKRLKVQLKRSKNDSKPY
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Molecular Weight
52kDa
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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 CELF1 (CUGBP Elav-like family member 1) protein is a key regulator of mRNA splicing, stability, and translation, playing vital roles in various biological processes, including muscle development and neuronal function. Abnormal expression or mutation of CELF1 has been implicated in several diseases, most notably myotonic dystrophy, a genetic disorder characterized by muscle wasting and myopathy. Research on CELF1 is crucial for understanding its regulatory mechanisms, the impact of alternative splicing on gene expression, and its potential role in disease pathogenesis. With the increasing recognition of the importance of RNA-binding proteins in post-transcriptional regulation, CELF1 has emerged as a significant focus of study. Investigating the structural and functional properties of CELF1, alongside its interactions with other splicing factors, is essential for elucidating its role in cellular processes and its contribution to disease. Moreover, the production of recombinant CELF1 protein facilitates the study of its biochemical properties and interactions in vitro, paving the way for potential therapeutic strategies targeting its dysregulation in diseases. Overall, the study of CELF1 and its recombinant forms not only enhances our understanding of RNA biology but also highlights the potential for novel interventions in RNA-related disorders.
