Analytical Data
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Gene name
SNRPD3
- Application
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Alternative Names
SNRPD3;Small nuclear ribonucleoProtein Sm D3
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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
P62318
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Expression Region
1-126aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMSIGVPIKVLHEAEGHIVTCETNTGEVYRG KLIEAEDNMNCQMSNITV TYRDGRVAQLEQVYIRGSKIRFLILPDMLK NAPMLKSMKNKNQGSGAGRGKAAILKAQVAARGRGRGMGRGNIFQ KRR
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Molecular Weight
16 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
SNRPD3, also known as Sm protein D3, is a crucial component of the spliceosome, the cellular machinery responsible for pre-mRNA splicing, a critical step in the maturation of eukaryotic mRNA. As a member of the Sm protein family, SNRPD3 plays a vital role in the assembly of the spliceosomal snRNPs (small nuclear ribonucleoproteins) and is involved in the regulation of gene expression. Research into SNRPD3 and its interactions has gained momentum due to its implications in various biological processes and diseases, including cancer. Understanding the structural and functional characteristics of SNRPD3, particularly through recombinant protein studies, provides insights into its role in splicing and potential contributions to alternative splicing mechanisms. The successful expression and purification of recombinant SNRPD3 protein allow researchers to investigate its biochemical properties, assess its interactions with RNA and other proteins, and explore its potential as a therapeutic target. Recent advances in methodologies for producing and characterizing this protein have opened new avenues for understanding how disruptions in the splicing process can lead to pathological conditions. Consequently, SNRPD3 serves not only as a fundamental component of RNA metabolism but also as a significant focus for research aimed at unraveling the complexities of gene regulation and therapeutic intervention strategies.
