Analytical Data
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基因名
ompC
- Application
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别名
ompC；SLAM；Signaling lymphocytic activation molecule
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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
P06996
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表达区间
22-367aa
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氨基酸序列
AEVYNKDGNKLDLYGKVDGLHYFSDNKDVDGDQTYMRLGFKGETQVTDQLTGYGQWEYQIQGNSAENENNSWTRVAFAGLKFQDVGSFDYGRNYGVVYDVTSWTDVLPEFGGDTYGSDNFMQQRGNGFATYRNTDFFGLVDGLNFAVQYQGKNGNPSGEGFTSGVTNNGRDALRQNGDGVGGSITYDYEGFGIGGAISSSKRTDAQNTAAYIGNGDRAETYTGGLKYDANNIYLAAQYTQTYNATRVGSLGWANKAQNFEAVAQYQFDFGLRPSLAYLQSKGKNLGRGYDDEDILKYVDVGATYYFNKNMSTYVDYKINLLDDNQFTRDAGINTDNIVALGLVYQF
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分子量
54.3 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
The ompC gene, which encodes a outer membrane porin protein in Escherichia coli, plays a crucial role in the bacterium's ability to regulate nutrient intake and maintain osmotic stability. Research on ompC recombinant protein has gained significant attention due to its potential applications in biotechnology and medicine. The porin protein facilitates the passive diffusion of small molecules and ions across the bacterial outer membrane, which is vital for E. coli’s survival in various environments. Understanding the structure and function of ompC can provide insights into bacterial adaptation mechanisms, antibiotic resistance, and the development of new antimicrobial strategies. Moreover, the expression and purification of ompC as a recombinant protein allow researchers to explore its biophysical properties and interactions with other cellular components. This can aid in the design of novel drugs targeting bacterial membranes. Additionally, ompC and its derivatives can be utilized in biosensing applications and as a model system for studying membrane protein folding and stability. Overall, the investigation of ompC recombinant protein carries significant implications for both fundamental science and practical applications in combating bacterial infections.
