Analytical Data
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Gene name
U2A/SNRPA
- Application
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Alternative Names
U1A; U1-A; Mud1; SNRP-A
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Species
Mouse
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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
Q62189
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Expression Region
Ala93~Lys287
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Molecular Weight
27kDa
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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
U2A/SNRPA, a crucial component of the splicing machinery in eukaryotic cells, plays a vital role in the regulation of pre-mRNA splicing. As a part of the U2 snRNP complex, U2A/SNRPA is involved in the recognition of the branch point sequence in introns, facilitating the assembly of the spliceosome. The study of U2A/SNRPA has garnered attention due to its implications in various cellular processes and its association with several diseases, including cancer and genetic disorders. The protein's structure and function have been extensively investigated, revealing insights into its interactions with RNA and other spliceosomal components. Additionally, the reconstitution of U2A/SNRPA in a controlled experimental setup allows researchers to probe its biochemical properties and functional dynamics comprehensively. Understanding the mechanisms governing U2A/SNRPA function is instrumental in deciphering the intricacies of RNA processing and may contribute to the development of targeted therapies for splicing-related diseases. Given the protein's significance in gene expression regulation, ongoing research aims to elucidate its precise role in splicing catalysis and its potential as a therapeutic target.
