Analytical Data
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Gene name
LUC7L3
- Application
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Alternative Names
Cisplatin resistance-associated-overexpressed protein;Luc7AOkadaic acid-inducible phosphoprotein OA48-18cAMP regulatory element-associated protein 1 ;CRE-associated protein 1 ;CREAP-1
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O95232
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Expression Region
1-79aa
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Molecular Weight
13.3 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
LUC7L3, or LUC7-like protein 3, is a member of the LUC7 family of proteins, which are critical for RNA processing and splicing in eukaryotic cells. Understanding LUC7L3 is crucial due to its involvement in the regulation of gene expression and its potential implications in various diseases, including cancer and neurodegenerative disorders. The protein plays a significant role in the formation of spliceosomal complexes, which are essential for the accurate removal of introns from pre-mRNA transcripts. Recent studies have highlighted LUC7L3's interactions with other splicing factors, contributing to its function in pre-mRNA splicing. Additionally, dysregulation of LUC7L3 has been linked to alternative splicing events that can lead to the expression of oncogenic isoforms or loss of tumor suppressor variants. Researchers are increasingly focused on isolating and characterizing LUC7L3 recombinant proteins to elucidate their molecular mechanisms of action and to explore their potential as therapeutic targets. Characterizing the structure-function relationship of LUC7L3 through recombinant protein studies could provide deeper insights into its role in splicing regulation and its involvement in pathological conditions. This research has broader implications for understanding cellular mRNA dynamics and the intricate regulatory networks governing gene expression in health and disease.
