Analytical Data
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基因名
U12
- Application
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别名
U12；KIAA1839；RBM40；RNP；RNA-binding region-containing Protein 3
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P52380
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表达区间
1-347aa
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氨基酸序列
MDTVIELSKLQFKGNASCTSTPTLKTARIMESAVTGITLTTSIPMIIIVVTTMILYHRVAKHNATSFYVITLFASDFVLMWCVFFMTVNRKQLFSFNRFFCQLVYFIYHAVCSYSISMLAIIATIRYKTLHRRKKTESKTSSTGRNIGILLLASSMCAIPTALFVKTNGMKKTGKCVVYISSKKAYELFLAVKIVFSFIWGVLPTMVFSFFYVIFCKALHDVTEKKYKKTLFFIRILLLSFLLIQIPYIAILICEIAFLYMPQNTCFWLARVEILQLIIRLMPQVHCFSNPLVYAFTGGELRNRFTACFQSFFPKTLCSTQKRKDSDASEHDQNSKSKASVEKNQPL
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分子量
42.6 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
U12 pre-mRNA is a component of the spliceosomal machinery responsible for the processing of non-canonical introns, distinct from the more common U2-type introns. The study of U12 and its associated proteins is crucial due to their implications in gene expression regulation and potential links to various diseases, including certain cancers and genetic disorders. U12 splicing is particularly interesting because it involves a unique set of snRNPs and spliceosomal components, making it a central focus for understanding the evolution of splicing mechanisms in eukaryotes. Recent advances in structural biology and computational methods have enabled researchers to dissect the functional roles of U12-associated proteins and their interactions within the spliceosome, thus opening up avenues for therapeutic interventions. Additionally, exploring U12-independent splicing pathways can provide insights into synthetic biology applications and biotechnological innovations. Understanding the functional dynamics of U12 spliceosomal components may lead to novel strategies for manipulating splicing events, advancing both basic research in molecular biology and applications in medical science.
