Analytical Data
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基因名
TXNL4B
- Application
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别名
TXNL4B；DIM2；Thioredoxin-like Protein 4B
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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
Q9NX01
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表达区间
1-149aa
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氨基酸序列
MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSMSFLLPKLTSKKEV DQAIKSTAEKVLVLRFGRDEDPVCLQLDDILSKTSSDLSKMAAIYLVDVD QTAVYTQYFDISYIPSTVFFFNGQHMKVDYGSPDHTKFVGSFKTKQDFID LIEVIYRGAMRGKLIVQSPIDPKNIPKYDLLYQDI
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分子量
21 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
TXNL4B, or Thioredoxin-Like 4B, is a member of the thioredoxin family known for its role in regulating various cellular processes, including redox homeostasis, cell proliferation, and apoptosis. Recent studies have highlighted TXNL4B's involvement in the response to cellular stress and its potential role in cancer progression and immune responses. As a redox-regulating protein, TXNL4B participates in the modulation of protein folding and maintenance of protein stability, making it crucial in various biological pathways. Researchers are increasingly focusing on TXNL4B for its potential as a therapeutic target, particularly in tumors where its expression is often dysregulated. The production of recombinant TXNL4B protein allows for detailed functional and structural studies, facilitating the understanding of its mechanisms of action and interactions with other cellular components. Investigating the properties of TXNL4B through recombinant techniques also enables the exploration of its potential applications in biotechnology and medicine. Given the growing interest in redox-related proteins, the recombinant study of TXNL4B may shed light on novel therapeutic strategies for diseases associated with oxidative stress and aberrant redox signaling. Through ongoing research, TXNL4B could emerge as an important biomarker or therapeutic target in the realm of oncology and beyond.
