Analytical Data
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Gene name
porB
- Application
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Alternative Names
porB；Protochlorophyllide reductase B. chloroplastic
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
E6MZM0
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Expression Region
20-331aa
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AA Sequence
DVTLYGTIKAGVETSRSVFHQNGQVTEVTTATGIVDLGSKIGFKGQEDLG NGLKAIWQVEQKASIAGTDSGWGNRQSFIGLKGGFGKLRVGRLNSVLKDT GDINPWDSKSDYLGVNKIAEPEARLISVRYDSPEFAGLSGSVQYALNDNA GRHNSESYHAGFNYKNGGFFVQYGGAYKRHHQVQEGLNIEKYQIHRLVSG YDNDALYASVAVQQQDAKLTDASNSHNSQTEVAATLAYRFGNVTPRVSYA HGFKGLVDDADIGNEYDQVVVGAEYDFSKRTSALVSAGWLQEGKGENKFV ATAGGVGLRHKF
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Molecular Weight
50 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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.
