Analytical Data
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Gene name
SNRPF
- Application
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Alternative Names
SMF; Sm-F; SNRP-F
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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
P62306
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Expression Region
Ser2~Glu86
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Molecular Weight
15kDa
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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
SNRPF (Small Nuclear Ribonucleoprotein Polypeptide F) is a critical component of the splicing machinery in eukaryotic cells, playing a pivotal role in the pre-mRNA splicing process. Research into SNRPF has gained importance due to its involvement in the regulation of gene expression and its potential implications in various diseases, including cancer and neurodegenerative disorders. Mutations and dysregulation of splicing factors like SNRPF can lead to aberrant splicing, contributing to the development and progression of several pathologies. Recent studies have begun to explore the structural and functional aspects of SNRPF, as well as its interactions with other proteins and RNA molecules within the spliceosome complex. Understanding the precise mechanisms by which SNRPF operates and its regulatory networks is essential for elucidating the intricate processes of gene expression. Furthermore, advancements in techniques such as CRISPR/Cas9 and high-throughput sequencing have enabled researchers to investigate SNRPF's roles more comprehensively, potentially leading to novel therapeutic targets for diseases associated with splicing abnormalities. Given its significance, SNRPF is being explored not only for its fundamental biological insights but also for its potential applications in biotechnology and medicine.
