Analytical Data
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Gene name
SNRPG
- Application
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Alternative Names
SNRPG;PBSCG;Small nuclear ribonucleoProtein G
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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
P62308
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Expression Region
1-76aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMSKAHPPELKKFMDKKLSLKLNGGRHVQGI LRGFDPFMNLVIDECVEMATSGQQNNIGMVVIRGNSIIMLEALERV
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Molecular Weight
11 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
Protein Description
SNRPG, or Small Nuclear Ribonucleoprotein G, is a crucial component of the spliceosome, a complex responsible for pre-mRNA splicing in eukaryotic cells. The importance of accurately splicing pre-mRNA cannot be overstated, as it directly influences gene expression and protein diversity. Abnormalities in this process have been linked to various diseases, including cancer and neurodegenerative disorders. Given its vital role in mRNA processing, studying SNRPG and its functions can provide deeper insights into the molecular mechanisms underlying these diseases. Researchers have focused on the structural and functional characterization of SNRPG, utilizing techniques like X-ray crystallography and cryo-electron microscopy to visualize its interactions within the spliceosome. Additionally, recombinant SNRPG protein has been produced to investigate its binding properties and role in splicing regulation. Understanding the dynamics of SNRPG can pave the way for developing therapeutic strategies targeting splicing abnormalities and enhancing cellular functions. The ongoing research aims to elucidate the intricate network of interactions involving SNRPG, thereby advancing our comprehension of RNA processing and its implications in health and disease.
