Analytical Data
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基因名
ompP2
- Application
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别名
ompP2; Outer membrane protein P2; OMP P2
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种属
Haemophilus influenzae
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表达系统
E. coli
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标签
N- His & C- Myc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q48216
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表达区间
21-360aa
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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
The ompP2 protein, derived from the outer membrane of bacteria, plays a crucial role in various biological processes and has garnered significant interest in the field of molecular biology and biotechnology. OmpP2 is part of the porin family, which facilitates the transport of small molecules across the bacterial outer membrane, thus impacting nutrient uptake, antibiotic resistance, and adaptation to environmental stresses. Research on ompP2 is essential for several reasons: it can provide insights into bacterial pathogenesis and survival mechanisms, serve as a potential target for novel antimicrobial therapies, and aid in the development of biosensors or drug delivery systems. Furthermore, the ability to recombinantly express and purify ompP2 allows for in-depth structural and functional analyses, contributing to our understanding of membrane proteins and their interactions. The exploration of ompP2 thus holds promise for both fundamental research in microbiology and practical applications in combating antibiotic resistance and enhancing biotechnological innovations. As a result, intensive studies aim to elucidate its structure-function relationship, revealing how this protein can be exploited for therapeutic and industrial purposes.
