Analytical Data
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Gene name
ptxA
- Application
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Alternative Names
ptxA；Phosphite import ATP-binding Protein PxtA
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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
Q7W2U8
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Expression Region
35-269aa
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AA Sequence
DDPPATVYRYDSRPPEDVFQNGFTAWGNNDNVLEHLTGRSCQVGSSNSAFVSTSSSRRYTEVYLEHRMQEAVEAERAGRGTGHFIGYIYEIRADNNFYGAASSYFEYVDTYGDNAGRILAGALATYQSEYLAHRRIPPENIRTVTRVYHNGITGETTTTEYPNLRYVSQQTRANTNPYTSRRSTASIVGTLVRMAPVTGACMARQAESPEAMAAWSERTGEAMVLVYYESIAYSF
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Molecular Weight
33.8 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
Related Products
Protein Description
The study of the ptxA gene, which encodes for the pertussis toxin (PT) production in Bordetella pertussis, has gained significant attention due to its role in the pathogenesis of whooping cough, a highly contagious respiratory disease. Understanding ptxA is crucial for vaccine development and improving therapeutic strategies. Pertussis toxin is a major virulence factor, contributing to bacterial adhesion and immune evasion. Recombinant expression of ptxA allows researchers to produce the pertussis toxin in a controlled environment, facilitating the investigation of its structure-function relationships. By utilizing various expression systems, including prokaryotic and eukaryotic platforms, scientists aim to better understand its immunogenic properties and potential as a vaccine component. Additionally, studies focusing on ptxA reconstitution help elucidate the molecular mechanisms underlying whooping cough, as well as the host's immune response to the toxin. Overall, the ongoing research on ptxA recombinant proteins is instrumental in advancing our knowledge of pertussis biology and enhancing public health interventions against this reemerging disease.
