Analytical Data
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Gene name
LSM4
- Application
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Alternative Names
LSM4;U6 snRNA-associated Sm-like Protein LSm4
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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
Q9Y4Z0
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Expression Region
1-139aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMLPLSLLKTAQNHPMLVELKNGETYNGHLV SCDNWMNINLREVICTSRDGDKFWRMPECYIRGSTIKYLRIPDEIIDMVK EEVVAKGRGRGGLQQQKQQKGRGMGGAGRGVFGGRGRGGIPGTGRGQPEK KPGRQAGKQ
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Molecular Weight
18 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
Related Products
Protein Description
The LSM4 protein, part of the LSm (like Sm) family, plays a critical role in RNA metabolism, particularly in the processes of mRNA splicing, degradation, and transport. Researching the LSM4 recombinant protein has garnered significant interest due to its essential functions in the life cycle of eukaryotic cells. LSM4 is known to form a heptameric complex with other LSm proteins, which is crucial for the assembly of RNA-processing complexes, such as the spliceosome and the telomerase complex. Understanding LSM4's interactions with RNA and other protein partners is vital for elucidating the molecular mechanisms that underlie gene expression regulation. Additionally, mutations or dysregulation of LSM4 have been implicated in various diseases, including cancer and neurodegenerative disorders, making it a potential target for therapeutic intervention. Thus, generating and characterizing recombinant LSM4 protein not only facilitates the study of its structural and functional properties but also supports the development of new strategies for disease management. The successful expression and purification of LSM4 in a laboratory setting allow researchers to perform detailed biochemical assays, structural analyses, and functional studies, ultimately contributing to a deeper understanding of RNA processing pathways and their implications in health and disease.
