Analytical Data
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Gene name
SNAP25
- Application
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Alternative Names
Super protein ;SUPSynaptosomal-associated 25KDA protein
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P60880
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Expression Region
1-206aa
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Molecular Weight
27.3 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
Shiga toxin 2B (Stx2B) is a variant of the Shiga toxin produced by certain pathogenic strains of Escherichia coli, particularly Shiga toxin-producing E. coli (STEC) such as O157:H7. This toxin is notorious for causing severe gastrointestinal disease, including hemorrhagic colitis and hemolytic uremic syndrome (HUS), which can lead to acute kidney failure, particularly in vulnerable populations like children and the elderly. The Stx2B subunit, part of the heterohexameric structure of the toxin, plays a crucial role in the binding of the toxin to host cells, facilitating the internalization of the enzymatically active Stx2A subunit. Research into recombinant Stx2B has gained momentum due to its potential applications in vaccine development, therapeutic interventions, and as a tool for understanding the pathogenesis of STEC infections. Recombinant techniques allow for the production of Stx2B in controlled settings, providing a safer model for studying its biological properties and interactions with the immune system. Furthermore, the incorporation of Stx2B into vaccine formulations could enhance immune responses, offering protective measures against STEC infections. Understanding the structural and functional aspects of Stx2B through recombinant technologies is essential for the development of effective diagnostics and therapeutics targeting Shiga toxin-related diseases. Hence, research focused on recombinant Stx2B holds significant promise for improving public health outcomes related to STEC infections and enhancing our comprehension of toxin-mediated cellular mechanisms.
