Product No. Toxin Weight (Da) Sequence Information Options 5250008 α-Conotoxin GI 1437,6 Da Sequence: [Cys2-Cys7, Cys3-Cys13 ]; H-Glu-Cys-Cys-Asn-Pro-Ala-Cys-Gly-Arg-His-Tyr-Ser-Cys-NH2 α-Conotoxin GI act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This conotoxin has been isolated from the venom of the cone snail Conus geographus. The higher affinity site for α-conotoxin GI is the α/Y site on mouse muscle-deriverd BC3H-1 receptor, and the other site (α/γsite) on nicotinic receptors from Torpedo californica electric organ. 5250041 ω-Conotoxin SO-3 2717,23 Da Sequence: [Cys2-Cys17, Cys9-Cys21, Cys16-Cys26 ]; H-Arg-Cys-Lys-Ala-Ala-Gly-Lys-Pro-Cys-Ser-Arg-Ile-Ala-Tyr-Asn-Cys-Cys-Thr-Gly-Ser-Cys-Arg-Ser-Gly-Lys-Cys-NH2 ω-conotoxins act at presynaptic membranes, they bind and block voltage-sensitive calcium channels (VSCC). This peptide selectively targets N-type voltage-sensitive calcium channels. Has no effect on R-type calcium currents, voltage-sensitive sodium currents, delayed rectifier potassium currents and transient outward potassium currents. Displays an analgesic potency similar to MVIIA in a range of acute and chronic pain models in rodents, but has less adverse effects compared with identical dosages of MVIIA injected intrathecally. 5250011 ω-Conotoxin MVIIC 2749,3 Da Sequence: [Cys1-Cys16, Cys8-Cys20, Cys15-Cys26 ]; H-Cys-Lys-Gly-Lys-Gly-Ala-Pro-Cys-Arg-Lys-Thr-Met-Tyr-Asp-Cys-Cys-Ser-Gly-Ser-Cys-Gly-Arg-Arg-Gly-Lys-Cys-NH2 ω-CgTx-MVIIC inhibits presynaptic Ca2+ channels, including the Ca2+ channels responsible for Ca2+ uptake by rat brain synaptosomes, the P-type Ca2+ channels in cerebellar Purkinje cells, and a significant fraction of ω-CgTx-GVIA-resistant currents in hippocampal CA1 neurons. ω-CgTx-MVIIC also presents an inhibition of ω-CgTx-GVIA-resistant depolarization-induced neurotransmetter release in cerebellar neurons of rats. 5250010 ω-Conotoxin MVIIA 2639,2 Da Sequence: [Cys1-Cys16, Cys8-Cys20, Cys15-Cys25 ]; H-Cys-Lys-Gly-Lys-Gly-Ala-Lys-Cys-Ser-Arg-Leu-Met-Tyr-Asp-Cys-Cys-Thr-Gly-Ser-Cys-Arg-Ser-Gly-Lys-Cys-NH2 ω-Conotoxin MVIIA has been isolated from the venom of the cone Conus magus. ω-Conotoxins act at presynaptic membranes, they bind and block voltage-sensitive calcium channels (VSCC). This toxin blocks N-type calcium channels (Cav2.2/CACNA1B). ω-Conotoxin MVIIA is available under the names Prialt by Neurex. It blocks acute pain in patients who no longer obtain relief from opiate drugs. It is 100 to 1000 times more potent than morphine. This toxin blocks calcium channels it disable nerves that transmit pain signals. 5250012 ω-Conotoxin GVIA 3037,3 Da Sequence: [Cys1-Cys16, Cys8-Cys19, Cys15-Cys26 ]; H-Cys-Lys-Ser-Hyp-Gly-Ser-Ser-Cys-Ser-Hyp-Thr-Ser-Tyr-Asn-Cys-Cys-Arg-Ser-Cys-Asn-Hyp-Tyr-Thr-Lys-Arg-Cys-Tyr-NH2 ω-Conotoxin GVIA has been isolated from the venom of the cone Conus geographus. ω-Conotoxins act at presynaptic membranes, they bind and block voltage-sensitive calcium channels (VSCC). 5250015 ρ-Conotoxin TIA 1195,6 Da Sequence: [Cys5-Cys11, Cys6-Cys19]; H-Phe-Asn-Trp-Arg-Cys-Cys-Leu-Ile-Pro-Ala-Cys-Arg-Arg-Asn-His-Lys-Lys-Phe-Cys-NH2 ρ-conotoxin TIA has been isolated from the venom of the cone Conus tulipa. Moreover this toxin reversibly inhibits α-1 adrenergic receptors (α-1B (ADRA1B) > α-1A (ADRA1A) = α-1D (ADRA1D)). This toxin is a competitive antagonist of α-1A- and α-1D-adrenoceptors and a non-competitive antagonist of α-1B-adrenoceptors. ρ-Conotoxin TIA has no effect on α-2 adrenergic receptors. But this compound potently inhibited contractions of vas deferens, spleen and aorta in response to noradrenaline. 5250030 α-Conotoxin MI 1493,7 Da Sequence: [Cys3-Cys8, Cys4-Cys14]; H-Gly-Arg-Cys-Cys-His-Pro-Ala-Cys-Gly-Lys-Asn-Tyr-Ser-Cys-NH2 α-Conotoxins MI has been isolated from the venom of the cone snail Conus magus. This conotoxin act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. α-Conotoxins MI blocks mammalian nAChR composed of a-1/δ subunits with high potency and α-1/γ with a low potency. 5250031 α-Conotoxin IMI 1351,6 Da Sequence: [Cys2-Cys8, Cys3-Cys12] ; H-Gly-Cys-Cys-Ser-Asp-Pro-Arg-Cys-Ala-Trp-Arg-Cys-NH2 α-Conotoxins IMI has been isolated from the venom of the cone snail Conus imperialis. a-conotoxins IMI act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin blocks mammalian neuronal nAChRs (α-3/β-2 > α-7 > α-3/β-4). Has no effect on nAChRs composed of α-2/β-2, α-3/β-2, α-4/β-2, α-2/β-4, α-3/β-4, or α-4/β-4 subunits. α-Conotoxins IMI acts voltage-independently. Is highly active against the neuromuscular receptor in frog. 5250009 α-Conotoxin GID 2184,9 Da Sequence: [Cys5-Cys11, Cys6-Cys19 ]; H-Ile-Arg-Asp-Gla-Cys-Cys-Ser-Asn-Pro-Ala-Cys-Arg-Val-Asn-Asn-Hyp-His-Val-Cys-OH α-Conotoxin GID act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This conotoxin has been isolated from the venom of the cone snail Conus geographus. This toxin reversibly blocks nAChRs (α-3/β-2 = α-7 >α-4/β-2). 5250050 Tertiapin-Q 2460,00 Da Sequence: [Cys3-Cys14, Cys5-Cys18 ]; H-Ala-Leu-Cys-Asn-Cys-Asn-Arg-Ile-Ile-Ile-Pro-His-Gln-Cys-Trp-Lys-Lys-Cys-Gly-Lys-Lys-NH2 Neurotoxin with presynaptic activity, that blocks the inwardly rectifying Kir1.1 (KCNJ1) and Kir3.1/3.4 (KCNJ3/KCNJ5) potassium channels with high affinity by binding to the M1-M2 linker region of these channels in a 1:1 stoichiometry. Tertiapin-Q also inhibits calcium-activated large conductance BK-type (KCNMA/KCNMB) potassium channels in a concentration-, and voltage-dependent manner, in addition to inhibiting Kir3.1/3.2 (KCNJ3/KCNJ6) heteromultimer potassium channels. It can prevent dose-dependently acetylcholine(ACh)-induced atrioventricular block in mammalian hearts. 5250038 SNX482 4495,08 Da Sequence: [Cys7-Cys21, Cys14-Cys26, Cys20-Cys33 ]; H-Gly-Val-Asp-Lys-Ala-Gly-Cys-Arg-Tyr-Met-Phe-Gly-Gly-Cys-Ser-Val-Asn-Asp-Asp-Cys-Cys-Pro-Arg-Leu-Gly-Cys-His-Ser-Leu-Phe-Ser-Tyr-Cys-Ala-Trp-Asp-Leu-Thr-Phe-Ser-Asp-OH SNX-482 has been isolated from the venom of the Spider Hysterocrates gigas (African tarantula). This toxin modulates the R-type current associated with the class a1E calcium channel Cav2.3 (CACNA1E). SNX-482 antagonizes channel activation by inducing a depolarizing shift in the activation potential, thus preventing the channel from undergoing normal membrane depolarization. SNX-482 acts rapidly and in a poorly reversible manner. 5250028 ShK Stichodactyla Toxin 4178,9 Da Sequence: [Cys3-Cys35, Cys12-Cys28, Cys17-Cys32]; H-Arg-Ser-Cys-Ile-Asp-Thr-Ile-Pro-Lys-Ser-Arg-Cys-Thr-Ala-Phe-Gln-Cys-Lys-His-Ser-Met-Lys-Tyr-Arg-Leu-Ser-Phe-Cys-Arg-Lys-Thr-Cys-Gly-Thr-Cys-OH ShK has been isolated from the venom of the sCarribean sea anemone Stoichactis helianthus. This toxin inhibits voltage-dependent potassium channels. Inhibits Kv1.3 (KCNA3) potently and also blocks Kv1.1 (KCNA1), Kv1.4 (KCNA4), and Kv1.6 (KCNA6) at subnanomolar concentrations. 5250037 Sarafotoxin-C 2515,8 Da Sequence: [Cys1-Cys15, Cys3-Cys11]; H-Cys-Thr-Cys-Asn-Asp-Met-Thr-Asp-Glu-Glu-Cys-Leu-Asn-Phe-Cys-His-Gln-Asp-Val-Ile-Trp-OH Sarafotoxin-C has been isolated from the venom of the Snaker Atractaspis engaddensis. This toxin presents a vasoconstrictor activity. This compound has a close structural homology to the endothelin family. Sarafotoxin-A causes cardiac arrest probably as a result of coronary vasospasm. LD50 is 0.3 mg/kg by intravenous injection for sarafotoxin-C. 5250036 Sarafotoxin-B 2563,9 Da Sequence: [Cys1-Cys15, Cys3-Cys11]; H-Cys-Ser-Cys-Lys-Asp-Met-Thr-Asp-Lys-Glu-Cys-Leu-Tyr-Phe-Cys-His-Gln-Asp-Val-Ile-Trp-OH Sarafotoxin-B has been isolated from the venom of the Snaker Atractaspis engaddensis. This toxin presents a vasoconstrictor activity. This compound has a close structural homology to the endothelin family. Sarafotoxin-A causes cardiac arrest probably as a result of coronary vasospasm. LD50 is 0.015 mg/kg by intravenous injection for Sarafotoxin-B. 5250035 Sarafotoxin-A 2500,9 Da Sequence: [Cys1-Cys15, Cys3-Cys11]; H-Cys-Ser-Cys-Lys-Asp-Met-Ser-Asp-Lys-Glu-Cys-Leu-Asn-Phe-Cys-His-Gln-Asp-Val-Ile-Trp-OH Sarafotoxin-A has been isolated from the venom of the Snaker Atractaspis engaddensis. This toxin presents a vasoconstrictor activity. This compound has a close structural homology to the endothelin family. Sarafotoxin-A causes cardiac arrest probably as a result of coronary vasospasm. LD50 is 0.015 mg/kg by intravenous injection for sarafotoxin-A. Infos anfordern Top 5250049 Psalmotoxin 1 PcTx1 7693,70 Da Sequence: [Cys3-Cys18, Cys10-Cys23, Cys17-Cys33 ]; H-Glu-Asp-Cys-Ile-Pro-Lys-Trp-Lys-Gly-Cys-Val-Asn-Arg-His-Gly-Asp-Cys-Cys-Glu-Gly-Leu-Glu-Cys-Trp-Lys-Arg-Arg-Arg-Ser-Phe-Glu-Val-Cys-Val-Pro-Lys-Thr-Pro-Lys-Thr-OH Potently and selectively blocks the H(+)-gated sodium channel ASIC1a (acid-sensitive ion channel 1a). The blockade is rapid and reversible. Psalmotoxin 1 loses its capacity to block ASIC1a as soon as this subunit is associated with another member of the family (ASIC2a or ASIC3). The toxin can distinguish between the two ASIC1 splice variants ASIC1a and ASIC1b. 5250048 Prototoxin 2 ProTx-II 3833,00 Da Sequence: [Cys2-Cys16, Cys9-Cys21, Cys15-Cys25 ]; H-Tyr-Cys-Gln-Lys-Trp-Met-Trp-Thr-Cys-Asp-Ser-Glu-Arg-Lys-Cys-Cys-Glu-Gly-Met-Val-Cys-Arg-Leu-Trp-Cys-Lys-Lys-Lys-Leu-Trp-OH Inhibits voltage-gated calcium and sodium channels (site 4). Inhibits activation by shifting the voltage-dependence of channel activation to more positive potentials. Potently inhibits all sodium channel subtypes tested (Nav1.2/SCN2A, Nav1.5/SCN5A, Nav1.7/SCN9A, and Nav1.8/SCN10A). Is approximately 15-fold more potent on Nav1.7/SCN9A than on Nav1.5/SCN5A channels. Acts on Cav3.1/CACNA1G, and interacts more weakly with the related T-Type channel Cav3.2/CACNA1H but potently inhibits the L-type calcium channel Cav1.2/CACNA1C. Binds to phospholipids. ProTx-II, a selective inhibitor of Nav1.7 sodium channels, blocks action potential propagation in nociceptors. 5250027 Maurotoxin 3613,0 Da Sequence: [Cys3-Cys24, Cys9-Cys29, Cys13-Cys19, Cys31-Cys34]; H-Val-Ser-Cys-Thr-Gly-Ser-Lys-Asp-Cys-Tyr-Ala-Pro-Cys-Arg-Lys-Gln-Thr-Gly-Cys-Pro-Asn-Ala-Lys-Cys-Ile-Asn-Lys-Ser-Cys-Lys-Cys-Tyr-Gly-Cys-NH2 Maurotoxin is a component of the venom of Scorpio maurus palmatus. This toxin is a member of the a-KTx6.2 scorpion toxin family. It blocks voltage-gated potassium channels (KV1.1/KCNA1, KV1.2/KCNA2, and KV1.3/KCNA3) and inhibits apamin-sensitive small conductance calcium-activated channels (SK channels), particularly KCa3.1(IKca1, SK4). 5250026 Maurocalcine 3858,5 Da Sequence: [Cys3-Cys17, Cys10-Cys21, Cys16-Cys32]; H-Gly-Asp-Cys-Leu-Pro-His-Leu-Lys-Leu-Cys-lys-Glu-Asn-Lys-Asp-Cys-Cys-Ser-Lys-Lys-Cys-Lys-Arg-Arg-Gly-Thr-Asn-Ile-Glu-Lys-Arg-Cys-Arg-OH Maurocalcine is a component of the venom of Scorpio maurus palmatus. It folds according to an inhibitor cysteine knot. It is a new member of the family of toxins acting on ryanodine receptors with an affinity in the 10 nM range. It induces an increase in channel opening probability accompanied with sudden transitions to long lasting subconductance states. It has also been characterized as a cell penetrating peptide and its pharmacological activity can be observed upon extracellular perfusion. 5250025 Margatoxin 4178,9 Da Sequence: [Cys7-Cys29, Cys13-Cys34, Cys17-Cys36]; H-Thr-Ile-Ile-Asn-Val-Lys-Cys-Thr-Ser-Pro-Lys-Gln-Cys-Leu-Pro-Pro-Cys-Lys-Ala-Gln-Phe-Gly-Gln-Ser-Ala-Gly-Ala-Lys-Cys-Met-Asn-Gly-Lys-Cys-Lys-Cys-Tyr-Pro-His-OH Margatoxin is a component of the venom of Scorpio Centruroides margaritatus.This toxin is potent selective inhibitor of voltage-dependent potassium channels such as Kv1.3. 5250024 Leiurotoxin 1 3423,1 Da Sequence: [Cys3-Cys21, Cys8-Cys26, Cys12-Cys28]; H-Ala-Phe-Cys-Asn-Leu-Arg-Met-Cys-Gln-Leu-Ser-Cys-Arg-Ser-Leu-Gly-Leu-Leu-Gly-Lys-Cys-Ile-Gly-Asp-Lys-Cys-Glu-Cys-Val-Lys-His-NH2 Scyllatoxin is a component of the venom of the Israeli scorpion Leiurus quinquestriatus hebraeus and has been reported to inhibit apamin binding to its receptor. Like apamin, it acts as a blocker of Ca2+ activated K+ channels in different cell types. 5250033 Kaliotoxin-1 4149 Da Sequence: [Cys8-Cys28, Cys14-Cys33, Cys18-Cys35]; H-Gly-Val-Glu-Ile-Asn-Val-Lys-Cys-Ser-Gly-Ser-Pro-Gln-Cys-Leu-Lys-Pro-Cys-Lys-Asp-Ala-Gly-Met-Arg-Phe-Gly-Lys-Cys-Met-Asn-Arg-Lys-Cys-His-Cys-Thr-Pro-Lys-NH2 Kaliotoxin-1 has been isolated from the venom of the Scorpion Androctonus mauretanicus mauretanicus. Kaliotoxin-1 is a potent inhibitor of large conductance calcium-activated potassium channels (BK-Ca). This toxin also binds to the dendrotoxin sensitive voltage-dependent potassium channel. It appears to block channel activity by a simple bimolecular inhibition process. Kaliotoxin-1 induces a transient period of fast flickering in the channel openings, followed by an almost complete blockade of the channel. Its binding affinity to rat brain synaptosomes is 5-fold higher than this of KTX-3. Binding of the toxin to the channel is associated with significant structural rearrangments in both molecules. 5250032 Imperatoxin A 3758,4 Da Sequence: [Cys3-Cys17, Cys10-Cys21, Cys16-Cys32]; H-Gly-Asp-Cys-Leu-Pro-His-Leu-Lys-Arg-Cys-Lys-Ala-Asp-Asn-Asp-Cys-Cys-Gly-Lys-Lys-Cys-Lys-Arg-Arg-Gly-Thr-Asn-Ala-Glu-Lys-Arg-Cys-Arg-OH Imperatoxin A has been isolated from the venom of the emperor Scorpion Pandinus imperator. Imperatoxin A is a strong agonist of ryanodine receptors (calcium release channels). This toxin induces voltage- and concentration-dependent subconductance states in both skeletal (RYR1 and RYR3) and cardiac (RYR2) ryanodine receptors by binding to a single, cytosolically accessible site different from the ryanodine binding site. Imperatoxin A enhances calcium release. 5250047 Huwentoxin-IV 4104,70 Da Sequence: [Cys2-Cys17, Cys9-Cys24,Cys16-Cys30]; H-Glu-Cys-Leu-Glu-Ile-Phe-Lys-Ala-Cys-Asn-Pro-Ser-Asn-Asp-Gln-Cys-Cys-Lys-Ser-Ser-Lys-Leu-Val-Cys-Ser-Arg-Lys-Thr-Arg-Trp-Cys-Lys-Tyr-Gln-Ile-NH2 Lethal neurotoxin. Acts selectively on tetrodotoxin-sensitive (TTX-S) voltage-gated sodium channels. IC50 is 30 nM in adult rat dorsal root ganglion neurons. 5250046 Huwentoxin-I 3750,45 Da Sequence: [Cys2-Cys17, Cys9-Cys22,Cys16-Cys29]; H-Ala-Cys-Lys-Gly-Val-Phe-Asp-Ala-Cys-Thr-Pro-Gly-Lys-Asn-Glu-Cys-Cys-Pro-Asn-Arg-Val-Cys-Ser-Asp-Lys-His-Lys-Trp-Cys-Lys-Trp-Lys-Leu-OH Lethal neurotoxin. Binds to the nicotinic acetylcholine receptor. Blocks neuromuscular transmission. Possess presynaptic activity that affects the release of neurotransmitters from autonomic nerve endings of both cholinergic and adrenergic neuroeffector junctions. Selectively inhibits N-type calcium channel and has only very weak effect on L-type calcium channel. Has virtually no effect on muscle sodium channels but are potent inhibitor of neuronal TTX-sensitive channels, especially Nav1.7 5250023 HsTx 1 4167,8 Da Sequence: [Cys3-Cys24, Cys9-Cys29, Cys13-Cys31, Cys19-Cys34]; H-Ala-Ser-Cys-Arg-Thr-Pro-Lys-Asp-Cys-Ala-Asp-Pro-Cys-Arg-Lys-Glu-Thr-Gly-Cys-Pro-Tyr-Gly-Lys-Cys-Met-Asn-Arg-Lys-Cys-Lys-Cys-Asn-Arg-Cys-NH2 HsTx 1 is a member of the a-KTx6 family of toxins active on voltage-gated K+ channels. It is one of the most potent toxins active on Kv1.3 channels (Kd close to 10 pM). It is also very active on Kv1.2 channels (Kd around 7 nM). It is however inactive on apamin-sensitive SK channels. 5250022 Hemitoxin 3899,2 Da Sequence: [Cys3-Cys24, Cys9-Cys29, Cys13-Cys19, Cys31-Cys34]; H-Ile-Lys-Cys-Thr-Leu-Ser-Lys-Asp-Cys-Tyr-Ser-Pro-Cys-Lys-Lys-Glu-Thr-Gly-Cys-Pro-Arg-Ala-Lys-Cys-Ile-Asn-Arg-Asn-Cys-Lys-Cys-Tyr-Gly-Cys-Ser-OH Hemitoxin has been isolated from the venom of the scorpion Hemiscorpius lepturus. This toxin blocks rat voltage-gated potassium channels Kv1.1 (KCNA1), Kv1.2 (KCNA2) and Kv1.3 (KCNA3) expressed in Xenopus oocytes. 5250020 GsMTx4 4093,9 Da Sequence: [Cys2-Cys17, Cys9-Cys23, Cys16-Cys30 ]; H-Gly-Cys-Leu-Glu-Phe-Trp-Trp-Lys-Cys-Asn-Pro-Asn-Asp-Asp-Lys-Cys-Cys-Arg-Pro-Lys-Leu-Lys-Cys-Ser-Lys-Leu-Phe-Lys-Leu-Cys-Asn-Phe-Ser-Phe-NH2 GsMTx4 has been isolated from the venom of the spider Grammostola rosea. This cationic hydrophobic polypeptide blocks mechanosensitive ion channels (also named strech-activated channels or SACs), without having effect on whole-cell voltage-sensitive currents. This Toxin acts by perturbing the interface between the channel and the lipid bilayer without necessarily being in physical contact with the channel. Also it affects the membrane motor of outer hair cells at low doses. It does not inhibit the potassium channel KvAP (from the archaeon Aeropyrum pernix). 5250021 Ergtoxin 4730,4 Da Sequence: [Cys4-Cys22, Cys10-Cys33, Cys19-Cys39, Cys23-Cys40]; H-Asp-Arg-Asp-Ser-Cys-Val-Asp-Lys-Ser-Arg-Cys-Ala-Lys-Tyr-Gly-Tyr-Tyr-Gln-Glu-Cys-Gln-Asp-Cys-Cys-Lys-Asn-Ala-Gly-His-Asn-Gly-Gly-Thr-Cys-Met-Phe-Phe-Lys-Cys-Lys-Cys-Ala-OH Ergtoxin has been isolated from the venom of the Mexican scorpion Centruroides noxius. This toxin blocks specifically the HERG potassium channel with an affinity close to 10 nM. 5250017 Conopeptide Y pl1 4092,1 Da Sequence: H-Ala-Arg-Phe-Leu-His-Pro-Phe-Gln-Tyr-Tyr-Thr-Leu-Tyr-Arg-Tyr-Leu-Thr-Arg-Phe-Leu-His-Arg-Tyr-Pro-Ile-Tyr-Tyr-Ile-Arg-Tyr-OH Conopeptide Y pl1 has been isolated from the venom of the cone Conus planorbis. This toxin is an antagonist of voltage-gated K+ channels belonging to the Kv1 subfamily. Conpeptide Y pl1 is selective for Kv1.6. Infos anfordern Top 5250016 Conantokin G 2264,2 Da Sequence: H-Gly-Glu-Gla-Gla-Leu-Gln-Gla-Asn-Gln-Gla-Leu-Ile-Arg-Gla-Lys-Ser-Asn-NH2 Conantokin G has been isolated from the venom of the cone Conus geographus. This toxin selectively inhibits NR2B subunits of N-methyl-D-aspartate (NMDA) receptor-mediated calcium influx in central nervous system neurons. Conantokin G induces sleep-like symptoms in young mice and hyperactivity in older mice(SERT). In this moment this compound is under phase II clinical trials under the name CGX-1007 by Cognetix Inc. It has been shown to be an effective antiepileptic agent in several animal models of seizur. 5250019 Chlorotoxin 3995,8 Da Sequence: [Cys2-Cys19, Cys5-Cys28, Cys16-Cys33, Cys20-Cys35]; H-Met-Cys-Met-Pro-Cys-Phe-Thr-Thr-Asp-His-Gln-Met-Ala-Arg-Lys-Cys-Asp-Asp-Cys-Cys-Gly-Gly-Lys-Gly-Arg-Gly-Lys-Cys-Tyr-Gly-Pro-Gln-Cys-Leu-Cys-Arg-OH Chlorotoxin is a chloride channel blocker which has been isolated from the venom of the scorpion Leiurus quinquestriatus. It has been shown to specifically bind to glioma cells and to inhibit their invasive potential. The toxin has recently been reported to bind to a protein complex on the surface of glioma cells containing several proteins implicated in glioma cell invasion. Gelatinase A (matrix metalloproteinase-2 (MMP2)) is one of the components present in this complex. The anti-invasive effect of chlorotoxin seems to be mediated by binding to and direct inhibition of gelatinase A, and its surface down-regulation. 5250044 APETx2 4567,00 Da Sequence: [Cys4-Cys37, Cys6-Cys30, Cys20-Cys38 ]; H-Gly-Thr-Ala-Cys-Ser-Cys-Gly-Asn-Ser-Lys-Gly-Ile-Tyr-Trp-Phe-Tyr-Arg-Pro-Ser-Cys-Pro-Thr-Asp-Arg-Gly-Tyr-Thr-Gly-Ser-Cys-Arg-Tyr-Phe-Leu-Gly-Thr-Cys-Cys-Thr-Pro-Ala-Asp-OH Potently and selectively blocks the H(+)-gated sodium channel ASIC3 (ACCN3). The blockade is rapid and reversible. Does not block isoform ASIC1a and isoform ASIC1b of ASIC1 (ACCN2), nor ASIC2 (ACCN1). It also inhibits heteromeric ASIC2b-ASIC3 channel, while it has less affinity for ASIC1b-ASIC3, ASIC1a-ASIC3, and no effect on the ASIC2a-ASIC3 channels. 5250018 Apamin 2027,3 Da Sequence: [Cys1-Cys11, Cys3-Cys15]; H-Cys-Asn-Cys-Lys-Ala-Pro-Glu-Thr-Ala-Leu-Cys-Ala-Arg-Arg-Cys-Gln-Gln-His-NH2 Apamin, which has been isolated from bee venom, is the smallest neurotoxic polypeptide known. It is the only polypeptide neurotoxin that passes the blood-brain barrier. It has several features in common with the snake and scorpion neurotoxins: like these, apamin is a low-molecular-weight basic peptide, and the molecule is crosslinked by disulfide bridges. 5250029 Agelenin 3818,5 Da Sequence: [Cys3-Cys17, Cys9-Cys22,Cys16-Cys32] - H-Gly-Gly-Cys-Leu-Pro-His-Asn-Arg-Phe-Cys-Asn-Ala-Leu-Ser-Gly-Pro-Arg-Cys-Cys-Ser-Gly-Leu-Lys-Cys-Lys-Glu-Leu-Ser-Ile-Trp-Asp-Ser-Arg-Cys-Leu-NH2 Agelenin has been isolated from the venom of the Agelenidae spider Agelena opulenta. This toxin suppresses the excitatory postsynaptic potentials possibly by blocking the presynaptic calcium channel. 5250042 μ-O-Conotoxin MrVIB 3463,28 Da Sequence: [Cys2-Cys20, Cys9-Cys25, Cys19-Cys30 ]; H-Ala-Cys-Ser-Lys-Lys-Trp-Glu-Tyr-Cys-Ile-Val-Pro-Ile-Leu-Gly-Phe-Val-Tyr-Cys-Cys-Pro-Gly-Leu-Ile-Cys-Gly-Pro-Phe-Val-Cys-Val-OH μ-O conotoxins block voltage-gated sodium channels. Has a preference for Nav1.4 (SCN4A) over Nav1.2 (SCN2A) sodium channels. Blocks Nav channels by interacting mainly with the C-terminal part of the pore loop of domain-3. Also blocks fast-inactivating calcium current. Blocks Nav1.8 (SCN10A) sodium channels and has potent and long-lasting local anesthetic effects. Can also block propagation of action potentials in A- and C-fibers in sciatic nerve as well as skeletal muscle in isolated preparations. Is under preclinical trial by Cognetix Inc under the name CGX-1002 as a local anesthetic agent. 5250043 μ-Conotoxin KIIIA 2104,00 Da Sequence: [Cys1-Cys9, Cys2-Cys15, Cys4-Cys16 ]; H-Cys-Cys-Asn-Cys-Ser-Ser-Lys-Trp-Cys-Arg-Asp-His-Ser-Arg-Cys-Cys-NH2 Neurotoxin with presynaptic activity, that blocks the inwardly rectifying Kir1.1 (KCNJ1) and Kir3.1/3.4 (KCNJ3/KCNJ5) potassium channels with high affinity by binding to the M1-M2 linker region of these channels in a 1:1 stoichiometry. Tertiapin-Q also inhibits calcium-activated large conductance BK-type (KCNMA/KCNMB) potassium channels in a concentration-, and voltage-dependent manner, in addition to inhibiting Kir3.1/3.2 (KCNJ3/KCNJ6) heteromultimer potassium channels. It can prevent dose-dependently acetylcholine(ACh)-induced atrioventricular block in mammalian hearts. Info request Top
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Chemicals, Finechemicals, Metal Compounds
