Analytical Data
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Gene name
SNRPG
- Application
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Alternative Names
SMG; Sm-G; SNRP-G
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Species
Human
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Source
E. coli
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Tag
N-His
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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
Met1~Val76
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Molecular Weight
12kDa
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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
SNRPG (small nuclear ribonucleoprotein G) is a crucial component of the spliceosomal machinery involved in pre-mRNA splicing. This protein plays a significant role in the assembly of splicesomes, facilitating the removal of introns and the joining of exons to produce mature mRNA. Research into SNRPG is driven by its potential implications in understanding various diseases, including cancers and genetic disorders, where splicing errors can lead to aberrant protein products and disrupted cellular functions. Additionally, SNRPG participates in the regulation of gene expression and contributes to the maintenance of RNA stability. Given its importance in cellular processes, recombinant SNRPG proteins are being utilized to elucidate the molecular mechanisms underlying splicing and to explore therapeutic strategies to rectify splicing defects. Advances in recombinant protein technology, including expression systems and purification methods, have enabled researchers to produce SNRPG in sufficient quantities for structural and functional studies. Understanding the detailed interactions of SNRPG with other spliceosomal components can provide insights into its role in splicing regulation and its broader impact on cellular health. This research not only deepens our understanding of RNA biology but may also lead to the development of targeted interventions for diseases linked to splicing anomalies.
