Recombinant Clostridium Botulinum Botulinum Neurotoxin Type C1 (BONT/C) Protein (His-SUMO)
Beta LifeScience
SKU/CAT #: BLC-04433P
Greater than 90% as determined by SDS-PAGE.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Clostridium botulinum N/A.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Clostridium botulinum N/A.
Recombinant Clostridium Botulinum Botulinum Neurotoxin Type C1 (BONT/C) Protein (His-SUMO)
Beta LifeScience
SKU/CAT #: BLC-04433P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.
Product Overview
| Description | Recombinant Clostridium Botulinum Botulinum Neurotoxin Type C1 (BONT/C) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment. |
| Purity | Greater than 90% as determined by SDS-PAGE. |
| Uniprotkb | P18640 |
| Target Symbol | P18640 |
| Synonyms | Botulinum neurotoxin type C; BoNT/C; Bontoxilysin-C1; BoNT/C1; Botulinum neurotoxin type C1) [Cleaved into: Botulinum neurotoxin C light chain; LC; EC 3.4.24.69); Botulinum neurotoxin C heavy chain; HC)] |
| Species | Clostridium botulinum |
| Expression System | E.coli |
| Tag | N-6His-SUMO |
| Target Protein Sequence | PITINNFNYSDPVDNKNILYLDTHLNTLANEPEKAFRITGNIWVIPDRFSRNSNPNLNKPPRVTSPKSGYYDPNYLSTDSDKDPFLKEIIKLFKRINSREIGEELIYRLSTDIPFPGNNNTPINTFDFDVDFNSVDVKTRQGNNWVKTGSINPSVIITGPRENIIDPETSTFKLTNNTFAAQEGFGALSIISISPRFMLTYSNATNDVGEGRFSKSEFCMDPILILMHELNHAMHNLYGIAIPNDQTISSVTSNIFYSQYNVKLEYAEIYAFGGPTIDLIPKSARKYFEEKALDYYRSIAKRLNSITTANPSSFNKYIGEYKQKLIRKYRFVVESSGEVTVNRNKFVELYNELTQIFTEFNYAKIYNVQNRKIYLSNVYTPVTANILDDNVYDIQNGFNIPKSNLNVLFMGQNLSRNPALRKVNPEN |
| Expression Range | 2-428aa |
| Protein Length | Partial |
| Mol. Weight | 64.9kDa |
| Research Area | Others |
| Form | Liquid or Lyophilized powder |
| Buffer | Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. |
| Reconstitution | Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%. |
| Storage | 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C. |
| Notes | Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week. |
Target Details
| Target 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. Is unique among characterized BoNTs in having 2 substrates, syntaxin (STX) and SNAP25. Precursor of botulinum neurotoxin C which unlike most BoNTs seems not to have a proteinaceous coreceptor, and instead recognizes 2 different complex polysialylated gangliosides found on neural tissue probably found in synaptic vesicles. 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 heavy chain (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. In vitro the whole toxin only has protease activity after reduction. Electrical stimulation increases uptake of toxin, presumably by transiently exposing a receptor usually found in eukaryotic target synaptic vesicles. Forms ion-conducting channels at around pH 6.1. Requires complex eukaryotic host polysialogangliosides for full neurotoxicity. Synaptic vesicle glycoproteins (SV2) do not seem to act as its receptor.; Has proteolytic activity. After translocation into the eukaryotic host cytosol, inhibits neurotransmitter release by acting as a zinc endopeptidase that cleaves syntaxin-1A/STX1A and syntaxin-1B/STX1B. Cleaves the '253-Arg-|-Ala-254' bond of STX1 and the '252-Arg-|-Ala-253' bond of STX2; also acts on syntaxin 3 (STX3) but not 4 (STX4). Cleaves the '198-Arg-|-Ala-199' bond of SNAP25. Recognizes the '93-Asn--Met-202' region of SNAP25.; Responsible for host epithelial cell transcytosis, host nerve cell targeting and translocation of light chain (LC) into eukaryotic 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 eukaryotic target cell surface. It simultaneously recognizes 2 polysialated gangliosides coreceptors in close proximity on host synaptic vesicles. 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 protect toxin prior to translocation. The TD inserts into synaptic vesicle membrane to allow translocation into the host cytosol. The C-terminal half of the HC (residues 864-1291) binds neurons in a dose-dependent manner. The C-terminal half of the HC (residues 863-1291) binds eukaryotic host gangliosides in the order GD1b > GT1b > GD1a > GM1a. Has 2 ganglioside binding sites; Sia-1 prefers a sia7 sialic acid and sugars within the ganglioside (GD1b > GT1b), whereas GBP2 recognizes a sia5 sialic acid (GT1b and GD1a). Both sites are required for HC to enter neurons, acting via different gangliosides. This suggests that 2 gangliosides serve as toxin receptors. Synaptic activity (depolarization with K(+)) increases uptake by neurons. Treatment of synaptosomes with proteinase K does not reduce HC binding, suggesting there is no protein receptor or it is protected from extracellular proteases. Decreases uptake and toxicity of whole BoNT/A, but also interferes with uptake of BoNT/E and BoNT/F. HC also binds phosphoinositides, which might play a role in membrane-binding. |
| Subcellular Location | [Botulinum neurotoxin type C]: Secreted.; [Botulinum neurotoxin C light chain]: Secreted.; [Botulinum neurotoxin C heavy chain]: Secreted. |
| Protein Families | Peptidase M27 family |
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