Name: Recombinant Clostridium botulinum Botulinum neurotoxin type A (botA), partial
Brand: CUSABIO
SKU: 400171CWV

Product Details

Purity

>85% (SDS-PAGE)

Target Names

botA

Uniprot No.

P0DPI1

Alternative Names

botA; bna; CBO0806; CLC_0862; Botulinum neurotoxin type A; BoNT/A; Bontoxilysin-A; BOTOX)

Species

Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A)

Protein Length

partial

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose, pH 8.0

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Customer Reviews and Q&A

■ Customer Reviews

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■ Q&A

Could you please provide sequence, pricing, availability and tag information for all available sizes?
Have you received any customer feedback about the activity of this protein?
Thank you.

Thanks for your inquiry.
Recombinant Clostridium botulinum Botulinum neurotoxin type A(botA) ,partial
CSB-EP400171CWV >> E.coli
Expression Region: 2-448aa; Partial, provide the Botulinum neurotoxin A light chain
Tag information:Tag type will be determined during the manufacturing process.
The expected tag is N-terminal 10xHis-tagged and C-terminal Myc-tagged.
Sequence:

PFVNKQFNYKDPVNGVDIAYIKIPNAGQMQPVKAFKIHNKIWVIPERDTFTNPEEGDLNPPPEAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYSTDLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGSYRSEELNLVIIGPSADIIQFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLEVDTNPLLGAGKFATDPAVTLAHELIHAGHRLYGIAINPNRVFKVNTNAYYEMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAKSIVGTTASLQYMKNVFKEKYLLSEDTSGKFSVDKLKFDKLYKMLTEIYTEDNFVKFFKVLNRKTYLNFDKAVFKINIVPKVNYTIYDGFNLRNTNLAANFNGQNTEINNMNFTKLKNFTGLFEFYKLLCVRGIITSKTKSLDKGYNK

Regarding the activity, sorry, we haven't tested the activity of this protein, so its activity is not 100% guaranteed.
In theory, we adopt affinity chromatography for puritication, which is purified under a very mild condition, it's very likely to be active.
We could recommend you to purchase a small size to have try.
Below is a literature for your reference: http://europepmc.org/abstract/MED/8294407

Target Background

Function

Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of the eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. Precursor of botulinum neurotoxin A which has 2 coreceptors; complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins of synaptic vesicles. Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them. Upon synaptic vesicle recycling the toxin is taken up via the endocytic pathway. When the pH of the toxin-containing endosome drops a structural rearrangement occurs so that the N-terminus of the HC forms pores that allows the light chain (LC) to translocate into the cytosol. Once in the cytosol the disulfide bond linking the 2 subunits is reduced and LC cleaves its target protein on synaptic vesicles, preventing their fusion with the cytoplasmic membrane and thus neurotransmitter release.; Has proteolytic activity. In vitro the whole toxin is reduced to release LC. After translocation into the eukaryotic host cytosol, LC hydrolyzes the 197-Gln-|-Arg-198 bond in SNAP25, blocking neurotransmitter release.; Responsible for host epithelial cell transcytosis, host nerve cell targeting and translocation of light chain (LC) into host cytosol. Composed of 3 subdomains; the translocation domain (TD), and N-terminus and C-terminus of the receptor-binding domain (RBD). The RBD is responsible for the adherence of the toxin to the cell surface. It simultaneously recognizes 2 coreceptors; polysialated gangliosides and synaptic vesicle glycoproteins SV2A, SV2B and SV2C in close proximity on host synaptic vesicles. The RBD specifically recognizes the N-linked glycan on 'Asn-559' of SV2A, SV2B and SV2C. Isolated HC binds to host synaptosomes, significantly decreases uptake and toxicity of whole BoNT/A. Binds ganglioside GD1a in vitro. The N-terminus of the TD wraps an extended belt around the perimeter of the LC, protecting Zn(2+) in the active site; it may also prevent premature LC dissociation from the translocation channel and to protect toxin prior to translocation. The TD inserts into synaptic vesicle membrane to allow translocation into the host cytosol.

Gene References into Functions

Structural and biochemical characterization of the protease domain of the mosaic botulinum neurotoxin type HA has been reported. PMID: 29688327
Inactivation of codY resulted in decreased expression of botA, encoding the neurotoxin. PMID: 25281376
These data help delineate why alpha-exosite binding is needed for SNAP-25 cleavage and also provide new insights into the extended lifetime observed for BoNT/A LC in vivo. PMID: 25295706
The importance of structural flexibility in the toxin's mechanism of survival and action is shown, an unmatched evolutionary trait from billion-year-old bacteria, also correlates with the long-lasting enzymatic activity of BoNT inside neuronal cells. PMID: 23746226
Constructed a deletion mutant of the binding domain of BoNT/A. The rBoNT/A-HCC at dose of 40 mug/mouse generated high IgG antibody titre with predominance of IgG1 subtype, but failed to protect animals against BoNT/A challenge. PMID: 22486648
BTX-A administration significantly reduces mechanical allodynia bilaterally and inhibits P2X3 purinergic receptor over-expression induced by lumbar ventral root transection. PMID: 21810163
BoNT/A impedes injury-activated neuronal function as displayed by upregulation of neuropeptide mRNA and a downregulation of proenkephalin mRNA in dorsal root ganglia. PMID: 21111791
A significant decrease is found in salivary flow rate at 1- and 3-month follow-up in the botulinum toxin A-treated group of children with sialorrhea and cerebral palsy. PMID: 21551374
BTX therapy, especially when associated with speech therapy, is efficacious in restoring phonation to laryngectomees who are unable to voice because of spasm of the paryngeal constrictor muscles. PMID: 21479612
Axonal transport of BTX-A, obligatory for its antinociceptive effects, occurs via sensory neurons and is directed to sensory nociceptive nuclei in the central nervous system. PMID: 21539899
[review] Successful retargeting of Bont-A can be used to treat medical conditions involving secretion from non-neuronal cells. PMID: 22047069
[review] The latest science and data about the clinical use of BONT is considered in a variety of applications of modern therapy in the treatment of spastic and dystonic conditions. PMID: 21244295
An indirect mechanism of afferent fiber modulation by botulinum toxin type A (BTX-A)is due to inhibition of the central loop reflex induced by BTX-A. PMID: 20493744
findings explain how botulinum neurotoxin serotype A light chain associates with SNAP-25 on the plasma membrane and provide a basis for N-terminal light chain (LC)/A cleavage of SNAP-25 within the SNARE complex PMID: 21378164
Peptides of Botulinum neurotoxin A is discussed in relation to their location in the 3-dimensional structure of the toxin molecule and their membrane receptor binding. PMID: 20571899
Axonal transport is a prerequisite for the antinociceptive action of botulinum toxin type A. The toxin's antinociceptive effect is independent of the sciatic nerve endings. PMID: 19732788
With the use of fluorescein-labeled dextran, we determined that the size of the channel is at least 24.2 A which is appropriate for the translocation of a protein of 50 kDa (the light chain of BoNT). PMID: 17216364
Review of retrograde axonal transport of catalytically active BoNT/A explains some of its effects at the level of central circuits. PMID: 19154335
Binding of neurotoxin A to the motor neuronal membrane activates neuritogenesis through as yet undetermined intracellular pathway(s), independent of its known action on vesicular release. PMID: 19372387

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Subcellular Location

[Botulinum neurotoxin A light chain]: Secreted. Host cytoplasm, host cytosol.; [Botulinum neurotoxin A heavy chain]: Secreted. Host cell junction, host synapse, host presynaptic cell membrane. Host cytoplasmic vesicle, host secretory vesicle, host synaptic vesicle membrane; Multi-pass membrane protein.

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Recombinant Clostridium botulinum Botulinum neurotoxin type A (botA), partial

Product Details

Customer Reviews and Q&A

Target Background

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