Analytical Data
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基因名
omp1A
- Application
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别名
Major outer membrane porin, serovar A; MOMP; ompA; omp1A; SA1/OT / Serovar A
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种属
Others
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表达系统
E. coli
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标签
N-SUMO;N-6*His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P23732
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表达区间
L23-F396
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蛋白长度
Full Length of Mature Protein
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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
OMP1A (Outer Membrane Protein 1A) is a significant protein found in the outer membrane of certain bacteria, particularly those of the genus *Neisseria*. Its study has gained attention due to its potential role in pathogenesis, immunogenic properties, and applicability in vaccine development. As a model for understanding outer membrane proteins, OMP1A can provide insights into bacterial resistance mechanisms and host-pathogen interactions. Research on OMP1A focuses on its structure, function, and immunogenicity, revealing how it may elicit immune responses and offer protective effects when presented as a recombinant protein. Advances in recombinant DNA technology have facilitated the expression and purification of OMP1A, enhancing our ability to investigate its properties and interactions. Additionally, due to the rising concern of antibiotic resistance, OMP1A has emerged as a promising target for the development of novel therapeutic strategies. Overall, the study of OMP1A reaffirms the importance of outer membrane proteins in medical microbiology and their potential in contributing to innovative solutions for bacterial infections.
