Recombinant Clostridium Botulinum Botulinum Neurotoxin Type B (BOTB) Protein (His-B2M)

Name: Recombinant Clostridium Botulinum Botulinum Neurotoxin Type B (BOTB) Protein (His-B2M)
Brand: Beta LifeScience
SKU: BLC-02385P
Availability: InStock

Greater than 85% 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 botB.

Collections: Fc receptors, Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Clostridium Botulinum Botulinum Neurotoxin Type B (BOTB) Protein (His-B2M) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P10844
Target Symbol	BOTB
Synonyms	botBBotulinum neurotoxin type B; BoNT/B; Bontoxilysin-B) [Cleaved into: Botulinum neurotoxin B light chain; LC; EC 3.4.24.69); Botulinum neurotoxin B heavy chain; HC)]
Species	Clostridium botulinum
Expression System	E.coli
Tag	N-6His-B2M
Target Protein Sequence	MPVTINNFNYNDPIDNNNIIMMEPPFARGTGRYYKAFKITDRIWIIPERYTFGYKPEDFNKSSGIFNRDVCEYYDPDYLNTNDKKNIFLQTMIKLFNRIKSKPLGEKLLEMIINGIPYLGDRRVPLEEFNTNIASVTVNKLISNPGEVERKKGIFANLIIFGPGPVLNENETIDIGIQNHFASREGFGGIMQMKFCPEYVSVFNNVQENKGASIFNRRGYFSDPALILMHELIHVLHGLYGIKVDDLPIVPNEKKFFMQSTDAIQAEELYTFGGQDPSIITPSTDKSIYDKVLQNFRGIVDRLNKVLVCISDPNININIYKNKFKDKYKFVEDSEGKYSIDVESFDKLYKSLMFGFTETNIAENYKIKTRASYFSDSLPPVKIKNLLDNEIYTIEEGFNISDKDMEKEYRGQNKAINKQAYEEISKE
Expression Range	1-427aa
Protein Length	Partial
Mol. Weight	63.3 kDa
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. Precursor of botulinum neurotoxin B which has 2 coreceptors; complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in 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. Binds to host peripheral neuronal presynaptic membranes via synaptotagmins 1 and 2 (SYT1 and SYT2). Toxin binds to the membrane proximal extra-cytoplasmic region of host SYT1 and SYT2 that is transiently exposed outside of cells during exocytosis; exogenous gangliosides enhance binding and subsequent uptake of toxin into host cells. Toxin uptake into neural cells requires stimulation (incubation with K(+) to stimulate SYT protein receptor exposure); subsequently the toxin colocalizes with its receptor in host cells with a concomitant decrease in target protein (synaptobrevin-2/VAMP2) immunoreactivity. Toxin uptake can be blocked by the appropriate synaptotagmin protein fragments and gangliosides in cell culture and in mice. BoNT/B is a 'coincidence detector'; it requires simultaneous binding to coreceptor GT1b and low pH to transform into a membrane-bound, oligomeric channel. Whole toxin only has protease activity after reduction which releases LC.; Has proteolytic activity. After translocation into the eukaryotic host cytosol, inhibits neurotransmitter release by acting as a zinc endopeptidase that cleaves the '76-Gln-\|-Phe-77' bond of synaptobrevin-2/VAMP2, blocking neurotransmitter release. In vitro the LC only has protease activity after reduction.; 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 N-terminus of the TD wraps an extended belt around the perimeter of the LC; it does not seem to protect the active site, but might prevent premature LC dissociation from the translocation channel and protect toxin prior to translocation. Has 2 coreceptors; complex gangliosides found primarily on neural tissue and host synaptotagmin-1 and -2 (SYT1 and SYT2) which bind simultaneously to adjacent but separate sites at the tip of the HC. HC alone partially prevents uptake of whole toxin by neural cells, and delays paralysis onset by 160%. Binding probably positions the TD for integration into the synaptic vesicle membrane. The HC forms channels at low pH that mediate transport of the light chain (LC) from the endocytic vesicle to the cytosol. Binds gangliosides GD1b and GT1b. Gangliosides are not only a coreceptor, but also required for uptake into nerve cells. HC alone binds to host receptor proteins SYT1 and SYT2. Interaction with SYT1 protein does not require SYT1 glycosylation. The HC C-terminus (approximately residues 1079-1291) interacts with host SYT2. Has higher affinity for SYT2 than SYT1. Significantly decreases uptake and toxicity of whole BoNT/B and BoNT/G.
Subcellular Location	[Botulinum neurotoxin type B]: Secreted. Host cell junction, host synapse, host presynaptic cell membrane.; [Botulinum neurotoxin B light chain]: Secreted. Host cytoplasm, host cytosol.; [Botulinum neurotoxin B 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.
Protein Families	Peptidase M27 family

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.