Analytical Data
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Gene name
speA
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简介
The speA protein plays a crucial role in catalyzing the transformation from arginine to agmatine. This enzymatic conversion highlights speA's significance in sustaining cellular metabolism and essential biological processes. By synthesizing agmatine, speA emerges as a key player in the intricate dance of molecular transformations that characterize fundamental cellular functions. speA Protein, Shewanella putrefaciens is the recombinant speA protein, expressed by E. coli , with tag free.
- Application
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Alternative Names
speA; Biosynthetic arginine decarboxylase; ADC
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Species
Others
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A4Y5Y9
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Expression Region
M1-S637
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Protein Length
Full Length
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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
The study of the recombinant protein speA (Streptococcus pyogenes exotoxin A) has gained significant attention due to its role as a virulence factor in the pathogenesis of Streptococcal infections. Streptococcus pyogenes, a bacterium responsible for various infections ranging from mild pharyngitis to severe conditions like necrotizing fasciitis and toxic shock syndrome, produces speA, which can function as a superantigen. This property allows speA to activate a large number of T cells, leading to an overwhelming immune response that can result in severe inflammatory reactions. The recombinant production of speA enables researchers to study its structure, function, and interaction with immune cells in vitro and in vivo, facilitating a deeper understanding of its mechanisms of action and potential therapeutic applications. Additionally, investigating the biochemical properties of speA can aid in the development of vaccine strategies and novel treatments against Streptococcus pyogenes infections. The insights gained from these studies can contribute to improved clinical outcomes and public health interventions targeting this pathogenic bacterium.
