Analytical Data
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基因名
lacI
- Application
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别名
lacI；LACI；TFPI1；Tissue factor pathway inhibitor
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种属
E.coli
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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
P03023
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表达区间
1-360aa
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氨基酸序列
MKPVTLYDVAEYAGVSYQTVSRVVNQASHVSAKTREKVEAAMAELNYIPNRVAQQLAGKQSLLIGVATSSLALHAPSQIVAAIKSRADQLGASVVVSMVERSGVEACKAAVHNLLAQRVSGLIINYPLDDQDAIAVEAACTNVPALFLDVSDQTPINSIIFSHEDGTRLGVEHLVALGHQQIALLAGPLSSVSARLRLAGWHKYLTRNQIQPIAEREGDWSAMSGFQQTMQMLNEGIVPTAMLVANDQMALGAMRAITESGLRVGADISVVGYDDTEDSSCYIPPLTTIKQDFRLLGQTSVDRLLQLSQGQAVKGNQLLPVSLVKRKTTLAPNTQTASPRALADSLMQLARQVSRLESGQC
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分子量
44.7 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
LacI is a pivotal regulatory protein in the lactose operon of Escherichia coli, acting as a transcriptional repressor that modulates the expression of genes involved in lactose metabolism. This protein binds to the operator region of the lac operon, preventing RNA polymerase from initiating transcription in the absence of lactose. The study of LacI has garnered considerable interest due to its role in understanding gene regulation mechanisms, as well as its potential applications in synthetic biology and biotechnology. Researchers have investigated the structural and functional dynamics of LacI, elucidating how allosteric changes occur upon binding of lactose or its analogs. These insights have enabled the design of engineered versions of LacI with modified regulatory properties, which can be harnessed for constructing genetic circuits. Additionally, LacI serves as a model for studying other regulatory proteins, inspiring research into complex gene interactions and the development of novel tools for genetic engineering. Overall, the investigation of LacI not only enhances our comprehension of fundamental biological processes but also opens avenues for innovative applications in gene therapy, metabolic engineering, and beyond.
