Analytical Data
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基因名
LMO4
- Application
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别名
Breast tumor autoantigen LIM domain only protein 4
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种属
Human
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表达系统
E. coli
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标签
N- GST
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P61968
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表达区间
1-165aa
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分子量
45 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
LMO4, also known as LIM domain-only protein 4, is a member of the LIM domain protein family, which is known for its role in cellular signaling and transcriptional regulation. Research has shown that LMO4 is involved in various biological processes, including neuronal development and differentiation, as well as the regulation of gene expression during embryogenesis. Its aberrant expression has been linked to several pathologies, including cancer, emphasizing the need for a better understanding of its functional mechanisms. The study of LMO4 recombinant protein has gained traction in recent years, as scientists aim to elucidate its structural properties, interaction partners, and functional roles in cellular contexts. This protein's unique structural domains provide a platform for potential therapeutic interventions, particularly in conditions where LMO4 dysregulation plays a critical role. By generating and characterizing LMO4 recombinant proteins, researchers aim to uncover insights into its pathways and explore its potential as a biomarker or target for therapeutic strategies, particularly in oncology. Understanding LMO4's biological functions and its interactions with other molecules could facilitate the development of innovative approaches to modulate its activity, thereby contributing to progress in cancer research and treatment.
