Analytical Data
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Gene name
LSM10
- Application
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Alternative Names
LSM10；U7 snRNA-associated Sm-like Protein LSm10
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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
Q969L4
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Expression Region
1-123aa
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AA Sequence
MAVSHSVKERTISENSLIILLQGLQGRVTTVDLRDESVAHGRIDNVDAFMNIRLAKVTYTDRWGHQVKLDDLFVTGRNVRYVHIPDDVNITSTIEQQLQIIHRVRNFGGKGQGRWEFPPKNCK
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Molecular Weight
30.1 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
The LSM10 protein is a crucial component of the lsm (like Sm) protein family, which plays a significant role in RNA metabolism, particularly in processes such as splicing, degradation, and the regulation of gene expression. LSM10 is known for its involvement in the assembly of small nuclear ribonucleoproteins (snRNPs), which are essential for pre-mRNA splicing in eukaryotic cells. As part of the Lsm complex, LSM10 interacts with various RNA molecules, facilitating their processing and stability. Research on LSM10 has gained momentum due to its potential implications in understanding various diseases, including neurodegenerative disorders and cancers, where disruptions in RNA regulation may occur. Additionally, LSM10's role in stress granule formation and its implications in cellular responses to environmental stressors further highlight its significance in cell biology. Understanding the structure, function, and interactions of LSM10 can provide insights into fundamental cellular mechanisms and may unveil novel therapeutic targets for RNA-related diseases. Recent studies utilizing advanced techniques such as cryo-electron microscopy and mass spectrometry have begun to elucidate the three-dimensional structure of LSM10 and its complexes, paving the way for more detailed functional analyses. Overall, the study of LSM10 not only enhances our understanding of RNA biology but also holds promise for contributing to the development of strategies to combat diseases associated with RNA dysregulation.
