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Below are the list of possible Beta/omega-theraphotoxin products. If you cannot find the target and/or product is not available in our catalog, please click here to contact us and request the product or submit your request for custom elisa kit production, custom recombinant protein production or custom antibody production. Custom ELISA Kits, Recombinant Proteins and Antibodies can be designed, manufactured and produced according to the researcher's specifications.


 Beta/omega-theraphotoxin-Tp1a ELISA Kit
 Beta/omega-theraphotoxin-Tp1a Recombinant
 Beta/omega-theraphotoxin-Tp1a Antibody
Also known as Beta/omega-theraphotoxin-Tp1a (Beta/omega-TRTX-Tp1a) (Protoxin-1) (ProTx-1) (ProTx-I) (ProTx1).
Inhibits voltage-gated calcium channels Cav3.1/CACNA1G, voltage-gated potassium channel
s Kv2.1/KCNB1 and all sodium channels tested (Nav1.2/SCN2A, Nav1.5/SCN5A, Nav1.7/SCN9A, and Nav1.8/SCN10A). Shifts the voltage-dependence of channel activation to more positive potentials. Most potent against Nav1.8/SCN10A.
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 Beta/omega-theraphotoxin-Tp2a ELISA Kit
 Beta/omega-theraphotoxin-Tp2a Recombinant
 Beta/omega-theraphotoxin-Tp2a Antibody
Also known as Beta/omega-theraphotoxin-Tp2a (Beta/omega-TRTX-Tp2a) (ProTx-II) (PT-II) (Protoxin-2) (ProTx-2) (ProTx2).
Blocks both tetrodotoxin-sensitive and tetrodotoxin-resistant human voltage-ga
ted sodium channels by shifting the voltage dependence of channel activation to more positive potentials. Inhibits Nav1.2/SCN2A, Nav1.3/SCN3A, Nav1.5/SCN5A, Nav1.6/SCN8A, Nav1.7/SCN9A, Nav1.8/SCN10A. Is significantly more potent against Nav1.7/SCN9A than the other Nav channel subtypes. Has no significant effect on Kv1.2/KCNA2, Kv1.3/KCNA3, Kv1.5/KCNA5, and Kv2.1/KCNB1 channels. Also inhibits Cav1.2/CACNA1C and Cav3.1/CACNA1G channels with an IC50 around 100 nM. Does not bind to the pharmacologically defined Nav channel sites 3 or 4. Neutralization of gating charges in the voltage sensor (S4) of domain II of Nav1.2/SCN2A prevents the effect of the toxin on gating current. Thus, it has been suggested that the toxin acts by trapping the voltage sensor of Nav channel domain II in the resting state, impeding outward gating movement of the IIS4 transmembrane segment of the channel. Binds to phospholipids.
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