Analytical Data
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Gene name
LSM6
- Application
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Alternative Names
LSM6U6 snRNA-associated Sm-like protein LSm6
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P62312
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Expression Region
1-80aa
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AA Sequence
MSLRKQTPSDFLKQIIGRPVVVKLNSGVDYRGVLACLDGYMNIALEQTEEYVNGQLKNKYGDAFIRGNNVLYISTQKRRM
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Molecular Weight
34.54 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 LSM6 (like Sm-like protein 6) is a member of the LSM (Like Sm) protein family, which plays a crucial role in various cellular processes, including RNA processing and regulation. Research into LSM6 has gained momentum due to its involvement in several fundamental biological mechanisms, such as splicing, stability, and degradation of RNA molecules. The protein is particularly important in the context of gene expression regulation and has been implicated in diverse physiological processes and diseases. Advances in molecular biology techniques have facilitated the characterization of LSM6 at the structural and functional levels, enabling scientists to unravel its interactions with RNA and other cellular components. Notably, mutations and dysregulation of LSM6 have been linked to various pathologies, including neurological disorders and cancer. Consequently, understanding the structure-function relationship of LSM6 through recombinant protein studies is essential for elucidating its biological roles and potential as a therapeutic target. The development of recombinant LSM6 proteins has opened avenues for in-depth investigations into its biochemical properties, interaction networks, and role in disease mechanisms, making it a significant focus of current research efforts in molecular and cellular biology.
