Analytical Data
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Gene name
LUC7L3
- Application
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Alternative Names
LUC7L3；RNPC7；RNA-binding Protein 25
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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
O95232
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Expression Region
1-79aa
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AA Sequence
MISAAQLLDELMGRDRNLAPDEKRSNVRWDHESVCKYYLCGFCPAELFTNTRSDLGPCEKIHDENLRKQYEKSSRFMKV
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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, a member of the LUC7 family of proteins, is known for its role in pre-mRNA splicing, influencing gene expression and mRNA maturation processes. Research on LUC7L3 has gained significance due to its involvement in various biological functions, including cell differentiation and proliferation, as well as its potential implications in several diseases such as cancer and neurodegenerative disorders. The protein contains specific domains that facilitate its interaction with splicing machinery and RNA substrates, making it a critical component in the spliceosome assembly. Recent studies have focused on elucidating its structural characteristics, functional mechanisms, and regulatory pathways, which could provide insights into its contributions to RNA processing and cellular homeostasis. Additionally, exploring LUC7L3's role in disease contexts could open avenues for therapeutic interventions and biomarker development. Given the complexity of gene regulation in eukaryotic cells, continued research into LUC7L3's molecular functions and interactions is essential for understanding its broader implications in health and disease.
