Analytical Data
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基因名
porB
- Application
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别名
porB；Protochlorophyllide reductase B. chloroplastic
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种属
Human
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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
E6MZM0
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表达区间
20-331aa
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氨基酸序列
DVTLYGTIKAGVETSRSVFHQNGQVTEVTTATGIVDLGSKIGFKGQEDLG NGLKAIWQVEQKASIAGTDSGWGNRQSFIGLKGGFGKLRVGRLNSVLKDT GDINPWDSKSDYLGVNKIAEPEARLISVRYDSPEFAGLSGSVQYALNDNA GRHNSESYHAGFNYKNGGFFVQYGGAYKRHHQVQEGLNIEKYQIHRLVSG YDNDALYASVAVQQQDAKLTDASNSHNSQTEVAATLAYRFGNVTPRVSYA HGFKGLVDDADIGNEYDQVVVGAEYDFSKRTSALVSAGWLQEGKGENKFV ATAGGVGLRHKF
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分子量
50 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
PorB, a protein derived from the outer membrane of Neisseria species, plays a crucial role in bacterial pathogenesis and immune system evasion. As a member of the porin family, PorB facilitates the transport of ions and small molecules across the bacterial membrane, contributing to the bacterium's survival in hostile environments. Given its significant involvement in immune response modulation, PorB has emerged as a target for vaccine development and therapeutic interventions, particularly against Neisseria meningitidis and Neisseria gonorrhoeae, which are responsible for severe meningitis and gonorrhea, respectively. Research on recombinant PorB aims to investigate its structural and functional properties, elucidate its interactions with host immune cells, and explore its potential as a vaccine candidate. Advances in recombinant DNA technology have enabled the production of PorB in heterologous systems, allowing for detailed studies of its immunogenicity and efficacy in eliciting protective immune responses. Understanding the mechanisms by which PorB exerts its effects on the immune system can pave the way for innovative strategies in combating Neisseria infections, ultimately contributing to the development of effective vaccines and therapies. Furthermore, the study of PorB serves as a model for exploring the broader implications of bacterial outer membrane proteins in infection biology.
