Analytical Data
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Gene name
botA
- Application
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Alternative Names
botA；KIAA1054；Synaptic vesicle glycoProtein 2C
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Species
E.coli
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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
P0DPI0
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Expression Region
1-436aa
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AA Sequence
MPFVNKQFNYKDPVNGVDIAYIKIPNVGQMQPVKAFKIHNKIWVIPERDTFTNPEEGDLNPPPEAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYSTDLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGSYRSEELNLVIIGPSADIIQFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLEVDTNPLLGAGKFATDPAVTLAHELIHAGHRLYGIAINPNRVFKVNTNAYYEMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAKSIVGTTASLQYMKNVFKEKYLLSEDTSGKFSVDKLKFDKLYKMLTEIYTEDNFVKFFKVLNRKTYLNFDKAVFKINIVPKVNYTIYDGFNLRNTNLAANFNGQNTEINNMNFTKLKNFTGLFEFYKLLCVRGIIT
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Molecular Weight
52.0 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
Botulinum toxin, produced by the bacteria *Clostridium botulinum*, is one of the most potent neurotoxins known, primarily affecting the nervous system and leading to Botulism, a serious illness characterized by muscle paralysis. The toxin comprises several serotypes, with botA being a subtype of particular interest due to its unique properties and potential applications in both medical and cosmetic fields. Research has shown that recombinant botA proteins can be synthesized using modern biotechnological methods, allowing for the exploration of their structure-function relationships and mechanisms of action. The ability to produce botA in a laboratory setting offers significant advantages over traditional extraction methods, which can be hazardous and inefficient. Furthermore, understanding the molecular details of botA and its interaction with neuromuscular junctions is critical not only for therapeutic developments, such as targeted treatments for spasticity and chronic pain but also for designing safer forms of the toxin for cosmetic procedures. Ongoing studies are focused on characterizing recombinant botA's pharmacological profiles, optimizing production techniques, and assessing its safety and efficacy in preclinical models. This research is pivotal for advancing our knowledge of botulinum neurotoxins and expanding their applications, ultimately benefiting both therapeutic and cosmetic domains.
