Analytical Data
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Gene name
LSM12
- Application
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Alternative Names
LSM12;Protein LSM12
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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
Q3MHD2
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Expression Region
1-195aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAAPPGE YFSVGSQVSC RTCQEQRLQG EVVAFDYQSK MLALKCPSSS GKPNHADILL INLQYVSEVE IINDRTETPP PLASLNVSKL ASKARTEKEE KLSQAYAISA GVSLEGQQLF QTIHKTIKDC KWQEKNIVVM EEVVITPPYQ VENCKGKEGS ALSHVRKIVE KHFRDVESQK ILQRSQAQQP QKEAALSS
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Molecular Weight
24 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 LSM12 protein, part of the LSM (Like-Sm) family, has garnered significant interest in the field of molecular biology due to its potential involvement in RNA metabolism and cellular stress responses. This family of proteins is characterized by their Sm-like (LSM) domain, which is crucial for RNA-binding and plays a vital role in the regulation of mRNA stability, splicing, and decay. LSM12, in particular, is thought to participate in the assembly of spliceosomal complexes and to influence the stability of specific mRNA targets. Recent studies have indicated its possible implications in oncogenesis and viral pathogenesis, highlighting the need to elucidate its functional mechanisms further. Research into LSM12 has revealed its expression patterns in various tissues, suggesting a role in developmental processes and cellular stress responses. Furthermore, the exploration of post-translational modifications of LSM12 can provide insights into its regulation and functional diversity under different physiological conditions. Understanding the biological functions and regulatory pathways of LSM12 not only enriches our comprehension of RNA processing and gene expression but also opens up potential therapeutic avenues for diseases linked to its dysfunction, making LSM12 a compelling focus for ongoing research in RNA biology and disease.
