Analytical Data
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Gene name
SNRPC
- Application
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Alternative Names
SNRP-C
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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
P09234
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Expression Region
Pro2~Arg159
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Molecular Weight
21kDa
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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
SNRPC, or the Small Nuclear Ribonucleoprotein Polypeptide C, is a crucial component of the spliceosome, the complex responsible for pre-mRNA splicing in eukaryotic cells. Research into SNRPC has gained momentum due to its significant role in gene expression regulation and potential implications in various diseases. Dysregulation of splicing processes can lead to the development of cancers, neurodegenerative disorders, and other genetic conditions. Understanding the structure and function of SNRPC is essential for elucidating how splicing machinery operates and how mutations might disrupt these processes. Recent studies have focused on characterizing SNRPC's interactions with RNA and other spliceosome components, utilizing techniques such as cryo-electron microscopy and mass spectrometry to reveal its functional dynamics. Additionally, the potential for SNRPC to serve as a therapeutic target in diseases associated with splicing anomalies has emerged, prompting investigations into small molecules that could modify its activity. Overall, the research surrounding SNRPC is pivotal not only for basic biological understanding but also for exploring innovative strategies in disease treatment and prevention.
