Analytical Data
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Gene name
SNRPD3
- Application
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Alternative Names
SMD3; SNRP-D3; snRNP core protein D3
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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
P62318
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Expression Region
Ser2~Arg126
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Molecular Weight
18kDa
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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, or small nuclear ribonucleoprotein D3, is a vital component of the spliceosome, the cellular machinery responsible for pre-mRNA splicing in eukaryotic cells. It plays a critical role in the assembly and functioning of the spliceosomal complexes, which are essential for the accurate processing of messenger RNA (mRNA). Dysregulation or mutations in SNRPD3 have been implicated in various diseases, including cancer and neurodegenerative disorders, highlighting its significance in gene expression regulation. Recent studies have focused on the recombinant expression of SNRPD3 to investigate its structural and functional properties, thereby enhancing our understanding of its role in RNA splicing. Additionally, the availability of recombinant SNRPD3 allows for the exploration of its interactions with other spliceosomal components and RNA molecules, facilitating the development of potential therapeutic targets. The investigation of SNRPD3 through recombinant protein studies is crucial for elucidating the complexities of mRNA splicing and its implications in health and disease.
