Analytical Data
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Gene name
U6A/SNRPA
- Application
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Alternative Names
(U1 snRNP A)(U1-A)(U1A)
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Species
Human
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Source
Baculovirus
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Tag
C- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P09012
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Expression Region
2-282aa
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Molecular Weight
36.8 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 U6A/SNRPA fusion protein has garnered significant interest in molecular biology due to its pivotal role in RNA splicing and its contribution to the understanding of spliceosome dynamics. U6A, a variant of the U6 small nuclear RNA (snRNA), is essential for the assembly and function of the spliceosome, a complex responsible for the removal of introns from pre-mRNA. SNRPA, a key protein involved in the recognition of U6 snRNA, facilitates its interaction with other spliceosomal components. The recombinant form of the U6A/SNRPA protein enables researchers to study the intricate mechanisms of splicing regulation, including the identification of protein-RNA interactions, the assessment of conformational changes during spliceosome assembly, and the examination of the impact of specific mutations on splicing fidelity. The investigation of this fusion protein not only advances our fundamental understanding of gene expression regulation but also has potential implications in understanding splicing-related diseases, providing a pathway for therapeutic development. Enhanced knowledge of U6A/SNRPA interactions may offer insights into the evolution of splicing mechanisms across different organisms, underscoring the importance of this research in both basic and applied biological sciences.
