Analytical Data
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Gene name
SNRPB2
- Application
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Alternative Names
SNRPB2;U2 small nuclear ribonucleoProtein B''
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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
P08579
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Expression Region
1-225aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMDIRPNHTIYINNMNDKIKKEELKRSLYAL FSQFGHVVDIVALKTMKMRGQAFVIFKELGSSTNALRQLQGFPFYGKPMR IQYAKTDSDIISKMRGTFADKEKKKEKKKAKTVEQTATTTNKKPGQGTPN SANTQGNSTPNPQVPDYPPNYILFLNNLPEETNEMMLSMLFNQFPGFKEV RLVPGRHDIAFVEFENDGQAGAARDALQGFKITPSHAMKITYAKK
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Molecular Weight
28 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
SNRPB2, a key component of the spliceosomal machinery, plays a critical role in the pre-mRNA splicing process, facilitating the removal of introns and the ligation of exons in eukaryotic cells. The protein is part of the Sm family, which forms the core of the spliceosomal small nuclear ribonucleoproteins (snRNPs). Given its essential function in gene expression regulation, the study of SNRPB2 has gained traction in the context of various cellular processes, including cell differentiation, proliferation, and response to cellular stress. Moreover, abnormalities in the function or expression of SNRPB2 have been linked to several human diseases, including cancers and neurodegenerative disorders. Therefore, understanding the biochemical properties of SNRPB2, including its structure, interactions with other spliceosomal components, and regulatory mechanisms, is crucial for unraveling its role in health and disease. Recent efforts have focused on the expression and purification of recombinant SNRPB2 to facilitate detailed functional studies and potential therapeutic investigations. By elucidating the molecular mechanisms underlying SNRPB2's activity, researchers hope to uncover novel avenues for targeted interventions in splicing-related disorders and enhance our understanding of post-transcriptional gene regulation.
