Analytical Data
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基因名
RBPMS
- Application
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别名
RBPMS;HERMES;RNA-binding Protein with multiple splicing
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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
Q93062
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表达区间
1-196aa
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氨基酸序列
MNNGGKAEKENTPSEANLQEEEVRTLFVSGLPLDIKPRELYLLFRPFKGYEGSLIKLTSKQPVGFVSFDSRSEAEAAKNALNGIRFDPEIPQTLRLEFAKANTKMAKNKLVGTPNPSTPLPNTVPQFIAREPYELTVPALYPSSPEVWAPYPLYPAELAPALPPPAFTYPASLHAQMRWLPPSEATSQGWKSRQFC
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分子量
28.8 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
RBPMS (RNA-binding protein with multiple splicing) is an important RNA-binding protein involved in various biological processes, including mRNA splicing, stability, and translation regulation. Its role has garnered significant attention in recent years due to its implication in diverse cellular functions and disease mechanisms, particularly in cancer. RBPMS participates in the regulation of gene expression and has been associated with mechanisms of tumorigenesis, where its expression levels can influence cell proliferation, differentiation, and apoptosis. Interestingly, RBPMS has been found to interact with various RNA molecules, modulating their metabolism and function. As a result, researchers have focused on the structure and function of RBPMS to understand its precise role at the molecular level. One key aspect of this research involves the production and characterization of recombinant RBPMS proteins, which serve as valuable tools for elucidating the protein's binding affinities, interaction partners, and functional implications in cellular pathways. Understanding the biochemical properties and functional mechanisms of RBPMS can provide insights into its potential as a therapeutic target and enhance our knowledge of RNA metabolism in health and disease contexts. In summary, the study of recombinant RBPMS not only enriches our understanding of RNA-binding proteins but also holds the promise for advancing therapeutic strategies against diseases where RBPMS plays a critical role.












