Analytical Data
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基因名
Trigger factor
- Application
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别名
(TF)(PPIase)
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种属
Escherichia coli O157:H7
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表达系统
E. coli
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标签
N- MBP & C- His-Avi
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P0A851
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表达区间
1-432aa
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分子量
96.0 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
Trigger factor (TF) is a highly conserved chaperone protein found in bacteria and organelles of eukaryotic cells, playing a vital role in protein folding and stabilization. It binds to nascent polypeptide chains emerging from the ribosome, preventing misfolding and aggregation, which is crucial in maintaining cellular protein homeostasis. Research into TF has gained momentum due to its potential implications in understanding protein synthesis and folding mechanisms, as well as its role in stress responses. The importance of TF extends beyond mere chaperoning; it has been implicated in various cellular processes, including assisting in the proper folding of multi-domain proteins and facilitating the assembly of protein complexes. Moreover, TF has been recognized for its potential in developing biotechnological applications, such as enhancing the yield of recombinant proteins in microbial systems. Recent studies have focused on elucidating the structural and functional properties of TF, exploring its interactions with various substrates, and understanding its regulation under physiological and stress conditions. As researchers aim to harness the capabilities of TF in different contexts, including therapeutics and industrial biotechnology, the exploration of recombinant TF continues to offer insights into its chaperone mechanics and potential applications in enhancing protein production and quality.
