Analytical Data
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Gene name
SNRPB
- Application
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Alternative Names
Small nuclear ribonucleoprotein-associated proteins B and B'. snRNP-B. Sm protein B/B'. Sm-B/B'. SmB/B'
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P14678
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Expression Region
1-80 aa
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AA Sequence
MTVGKSSKMLQHIDYRMRCILQDGRIFIGTFKAFDKHMNLILCDCDEFRKIKPKNSKQAEREEKRVLGLVLLRGENLVSM
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Molecular Weight
34.54 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
The SNRPB (Small Nuclear Ribonucleoprotein B) protein is a crucial component of the spliceosome, a complex responsible for the post-transcriptional modification of precursor messenger RNA (pre-mRNA) in eukaryotic cells. It plays a vital role in the splicing process, where introns are removed and exons are joined to produce mature mRNA, which subsequently directs protein synthesis. Dysregulation of SNRPB expression or function is implicated in various diseases, including cancers and neurodegenerative disorders, making it an important target for research. Recent studies have focused on characterizing the structural and functional properties of SNRPB, as well as its interactions with other spliceosomal factors. Understanding the mechanistic role of SNRPB in pre-mRNA splicing and its regulatory pathways is essential for elucidating the molecular basis of splicing-related diseases. Moreover, the development of SNRPB recombinant proteins has facilitated the investigation of its function and interaction dynamics, providing insights that could lead to novel therapeutic strategies for conditions arising from splicing errors. This research area holds the promise of uncovering new molecular targets and enhancing our comprehension of gene expression regulation at the translational level.
