Analytical Data
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Gene name
snrnp35
- Application
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Alternative Names
(U11/U12 snRNP 35 kDa protein)(U1 snRNP-binding protein homolog)
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Species
Zebrafish
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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
Q4KMD3
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Expression Region
1-208aa
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Molecular Weight
28.7 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
SNRNP35, or Small Nuclear Ribonucleoprotein U5 Subunit 35, is an essential component of the spliceosomal machinery responsible for pre-mRNA splicing in eukaryotic cells. This protein plays a crucial role in the assembly and function of the spliceosome, a complex that removes introns from precursor mRNA transcripts and ensures the generation of mature mRNA. The study of SNRNP35 has garnered interest due to its involvement in various cellular processes and potential links to diseases. Aberrations in splicing mechanisms have been implicated in several pathologies, including cancer and genetic disorders. Understanding the structure, function, and interactions of SNRNP35 can provide valuable insights into the regulation of gene expression and the implications of spliceosome dysfunction. Recent advances in protein engineering allow for the synthesis of recombinant SNRNP35, facilitating detailed biochemical and biophysical studies. These studies aim to elucidate the molecular mechanisms underlying splicing and to explore potential therapeutic strategies targeting splicing pathways. As researchers continue to investigate the role of SNRNP35 within the spliceosome, its importance in maintaining cellular homeostasis and its potential as a biomarker or therapeutic target in splicing-related diseases remain key areas of focus in molecular biology and biotechnology.
