Analytical Data
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Gene name
SNRNP25
- Application
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Alternative Names
SNRNP25;C16orf33;U11/U12 small nuclear ribonucleoProtein 25 kDa Protein
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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
Q9BV90
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Expression Region
1-132aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMDVFQEGLAMVVQDPLLCDLPIQVTLEEVN SQIALEYGQAMTVRVCKMDGEVMPVVVVQSATVLDLKKAI QRYVQLKQEREGGIQHISWSYVWRTYHLTSAGEKLTEDRKKLRDYGIRNR DEVSFIKKLRQK
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Molecular Weight
17 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
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Protein Description
SNRNP25, or small nuclear ribonucleoprotein-related protein 25, has emerged as a significant focus in molecular biology due to its essential roles in RNA splicing and gene regulation. This protein is a component of the spliceosome, a complex responsible for the removal of introns from pre-mRNA, thus playing a crucial part in the maturation of messenger RNA (mRNA) and overall gene expression regulation. Given the fundamental importance of splicing in the synthesis of functional proteins, abnormalities in SNRNP25 function are implicated in various diseases, including cancer and genetic disorders. Recent studies have highlighted its involvement in the regulation of alternative splicing, which can influence cellular responses to various stimuli and developmental processes. The investigation of SNRNP25 as a recombinant protein allows for detailed studies of its structural and functional properties, aiding in the understanding of its roles within the spliceosome and its potential as a therapeutic target. Moreover, the generation of SNRNP25 recombinant proteins provides a valuable resource for high-throughput screening assays aimed at identifying small molecules that could modulate splicing pathways, potentially offering new strategies for the treatment of splicing-related diseases. Understanding the intricate mechanisms behind SNRNP25 function will not only shed light on fundamental biological processes but also pave the way for innovative approaches in drug development and personalized medicine. As such, research on SNRNP25 reaffirms its relevance in both basic and applied biomedical sciences.
