Analytical Data
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基因名
botF
- Application
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别名
botF；SYB2；Vesicle-associated membrane Protein 2
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种属
Clostridium
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P30996
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表达区间
1-436aa
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氨基酸序列
MPVAINSFNYNDPVNDDTILYMQIPYEEKSKKYYKAFEIMRNVWIIPERNTIGTNPSDFDPPASLKNGSSAYYDPNYLTTDAEKDRYLKTTIKLFKRINSNPAGKVLLQEISYAKPYLGNDHTPIDEFSPVTRTTSVNIKLSTNVESSMLLNLLVLGAGPDIFESCCYPVRKLIDPDVVYDPSNYGFGSINIVTFSPEYEYTFNDISGGHNSSTESFIADPAISLAHELIHALHGLYGARGVTYEETIEVKQAPLMIAEKPIRLEEFLTFGGQDLNIITSAMKEKIYNNLLANYEKIATRLSEVNSAPPEYDINEYKDYFQWKYGLDKNADGSYTVNENKFNEIYKKLYSFTESDLANKFKVKCRNTYFIKYEFLKVPNLLDDDIYTVSEGFNIGNLAVNNRGQSIKLNPKIIDSIPDKGLVEKIVKFCKSVIPRK
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分子量
51.6 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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 botulinum toxin, particularly its recombinant proteins, has garnered significant attention due to the pathogenic effects of Clostridium botulinum, the bacterium responsible for botulism. This neurotoxin is one of the most potent toxins known, functioning by inhibiting neurotransmitter release, leading to muscle paralysis. Understanding the mechanisms of botulinum toxin has critical implications not only for medical applications, such as the treatment of various neuromuscular disorders and cosmetic procedures, but also for developing effective vaccines and therapeutics against botulism. Recombinant proteins derived from botulinum toxin provide a valuable tool for studying its structure-function relationships, enhancing safety and efficacy in therapeutic uses. Advances in genetic engineering and molecular biology enable the production of modified forms of the toxin that retain biological activity while minimizing adverse effects. Additionally, by exploring the biochemical pathways and receptor interactions of these recombinant proteins, researchers aim to elucidate the toxin's mode of action. This knowledge is crucial for designing better antidotes and for potential applications in pharmacology and biotechnology, further emphasizing the relevance of botulinum toxin research in both clinical and industrial contexts. The ongoing exploration of botF recombinant proteins holds promise for innovative treatments and deeper insights into neurobiology.
