Analytical Data
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基因名
U6A/SNRPA
- Application
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别名
(U1 snRNP A)(U1-A)(U1A)
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种属
Human
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表达系统
Baculovirus
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标签
C- His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P09012
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表达区间
2-282aa
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分子量
36.8 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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.
