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작성일 : 13-05-29
[Smartox Biotechnology] 화학합성의 Calcium Channel Blocker Peptide Toxin(1)
ω-agatoxin IVA / ω-CONOTOXIN GVIA(Omega conotoxin GVIA) / ω-Conotoxin MVIIC(Omega conotoxin MVIIC) / SNX482
 
화학합성의 각종 Calcium Channel Blocker Peptide Toxin (1)
 
Calcium channel 연구에 유용한 유독 생물 유래의 합성 peptide toxin 입니다. 화학합성 peptide이기 때문에
endotoxin 오염의 걱정이 없습니다.
 
 
ω-agatoxin IVA
 
ω-agatoxin IVA is a peptide originally isolated from funnel web-spider venom Agelenopsis aperta. This peptide is a specific
blocker of P/Q-type calcium channel (Cav2.1). It has been reported that ω-agatoxin IVA is a potent blocker of voltage-
gated calcium channels in insect and vertebrate central neurons. The binding site for ω-agatoxin IVA has been localized in
part to the extracellular S3–S4 loop in repeat IV of the α-1A Ca2+ channels, which is proximal to the S4 sensor domain. This is coherent with its functional effect (no pore-blocking activity, but gating modifier by a shift of channel activation
towards more depolarized potentials). This makes this toxin a voltage-dependent blocker of P/Q calcium channels.
 
Details
AA sequence:
 
H-Cys1-Lys-Gly-Lys-Gly-Ala-Pro-Cys8-Arg-Lys-Thr-Met-Tyr-Asp-Cys15-Cys16-Ser-Gly-Ser-Cys20-
Gly-Arg-Arg-Gly-Lys-Cys26-NH2
 
(Disulfide bonds between Cys1-Cys16, Cys8-Cys20, and Cys15-Cys26)
Length (aa):
 
26
Formula:
C106H178N40O32S7
Molecular Weight:
 
2750.2 Da
Appearance:
 
White lyophilized solid
Solubility:
 
Water and saline buffer
CAS number:
147794-23-8
Source:
 
Synthetic
Purity rate:
 
> 97%
 
References
1. Mintz I.M., et al. (1992) P-type calcium channels blocked by the spider toxin omega-Aga-IVA. Nature . PubMed link
2. Bourinet E, et al. (1999) Splicing of alpha 1A subunit gene generates phenotypic variants of P- and Q-type calcium
   channels. Nat Neurosci. PubMed link
3. Adams ME. (2004) Agatoxins: ion channel specific toxins from the American funnel web spider, Agelenopsis aperta.
   Toxicon. PubMed link
4. Doering CJ, Zamponi GW. (2003) Molecular pharmacology of high voltage-activated calcium channels. J Bioenerg
   Biomembr. PubMed link
5. Winterfield JR, Swartz KJ. (2000) A hot spot for the interaction of gating modifier toxins with voltage-dependent ion
   channels. J Gen Physiol. PubMed link
6. King GF. (2007) Modulation of insect Ca(v) channels by peptidic spider toxins. Toxicon. PubMed link
7. Wicher D, Penzlin H. (1998) omega-Toxins affect Na+ currents in neurosecretory insect neurons. Receptors Channels.
8. Wicher D, Penzlin H. (1997) Ca2+ currents in central insect neurons: electrophysiological and pharmacological
   properties. J Neurophysiol. PubMed link
 
 
ω-CONOTOXIN GVIA / Omega conotoxin GVIA
 
ω-conotoxin GVIA has been isolated from the venom of the cone Conus geographus. Omega-conotoxin GVIA acts at
presynaptic membranes. It binds and blocks specifically Cav2.2 channel with an ED50 of 68pM.
 
Details
AA sequence:
 
H-Cys1-Lys-Ser-Hyp-Gly-Ser-Ser-Cys8-Ser-Hyp-Thr-Ser-Tyr-Asn-Cys15-Cys16-Arg-Ser-Cys19-
Asn-Hyp*-Tyr-Thr-Lys-Arg-Cys26-Tyr-NH2  (Hyp: hydroxyproline)
 
(Disulfide bonds between Cys1-Cys16, Cys8-Cys9, and Cys15-Cys26)
Length (aa):
 
27
Formula:
C120H182N38O43S6
Molecular Weight:
 
3036.05 Da
Appearance:
 
White lyophilized solid
Solubility:
 
Water and saline buffer
CAS number:
106375-28-4
Source:
 
Synthetic
Purity
 
> 95%
 
References
1. Lew, M. J., et al. (1997) Structure-function relationships of omega-conotoxin GVIA. Synthesis, structure, calcium
   channel binding, and functional assay of alanine-substituted analogues, J Biol Chem. PubMed link
2. Seiji Ichida, et al. (2005) Characteristics of Omega-conotoxin GVIA and MVIIC Binding to Cav 2.1 and Cav 2.2
   Channels Captured by Anti-Ca2+ Channel Peptide Antibodies, Neurochemical Research. PubMed link
3. Schroeder Cl., et al. (2006) N-type calcium channel blockers: novel therapeutics for the treatment of pain. Med Chem.
 
 
ω-Conotoxin MVIIC / Omega conotoxin MVIIC
 
ω-conotoxin MVIIC has been isolated from the venom of the cone Conus magus. ω-conotoxin 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-conotoxin GVIA-resistant currents in hippocampal CA1
neurons. ω-conotoxin MVIIC also presents an inhibition of ω-conotoxin GVIA-resistant depolarization-induced
neurotransmitter release in cerebellar neurons of rats.
 
Details
AA sequence:
 
H-Cys1-Lys-Gly-Lys-Gly-Ala-Pro-Cys8-Arg-Lys-Thr-Met-Tyr-Asp-Cys15-Cys16-Ser-Gly-Ser-Cys20-
Gly-Arg-Arg-Gly-Lys-Cys26-NH2
 
(Disulfide bonds between Cys1-Cys16, Cys8-Cys20, and Cys15-Cys26)
Length (aa):
 
26
Formula:
C106H178N40O32S7
Molecular Weight:
 
2750.2 Da
Appearance:
 
White lyophilized solid
Solubility:
 
Water and saline buffer
CAS number:
147794-23-8
Source:
 
Synthetic
Purity rate:
 
> 97%
 
References
1. Hillyard, D. R., et al. (1992) A new Conus peptide ligand for mammalian presynaptic Ca2+ channels, Neuron.
2. Woppmann A, (1994) Calcium channel subtypes in rat brain: biochemical characterization of the high-affinity receptors
   for omega-conopeptides SNX-230 (synthetic MVIIC), SNX-183 (SVIB), and SNX-111 (MVIIA), Mol Cell Neurosci.
3. Grantham CJ, (1994) Omega-conotoxin MVIIC reve rsibly inhibits a human N-type calcium channel and calcium influx
   into chick synaptosomes, Neuropharmacology. PubMed link
 
 
SNX482
 
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 α1E calcium channel (Cav2.3 from the CACNA1E gene). 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 maintains its effect.
 
Details
AA sequence:
 
H-Gly-Val-Asp-Lys-Ala-Gly-Cys7-Arg-Tyr-Met-Phe-Gly-Gly-Cys14-Ser-Val-Asn-Asp-Asp-Cys20-
Cys21-Pro-Arg-Leu-Gly-Cys26-His-Ser-Leu-Phe-Ser-Tyr-Cys33-Ala-Trp-Asp-Leu-Thr-Phe-Ser-
Asp-OH
 
(Disulfide bridges: Cys7-Cys21, Cys14-Cys26, and Cys20-Cys33)
Length (aa):
 
41
Formula:
C192H274N52O60S7
Molecular Weight:
 
4496.42 Da
Appearance:
 
White lyophilized solid
Solubility:
 
Water and saline buffer
CAS number:
203460-30-4
Source:
 
Synthetic
Purity rate:
 
> 95 %
 
References
1. Arroyo G, et al. (2003) SNX482 selectively blocks P/Q Ca2+ channels and delays the inactivation of Na+ channels
   of chromaffin cells, Eur J Pharmacol. PubMed link
2. Bourinet, E., et al. (2001) Interaction of SNX482 with domains III and IV inhibits activation gating of alpha(1E)
   (Ca(V)2.3) calcium channels, Biophys. PubMed link
3. Newcomb, R., et al. (1998) Selective peptide antagonist of the class E calcium channel from the venom of the
   tarantula Hysterocrates gigas, Biochemistry. PubMed link
 
 
Ordering informations
 
Catalog No.
Product Name
Size
 11AGA001
ω-agatoxin IVA
 0.1mg, 0.5mg & 1.0mg
08CON003
ω-CONOTOXIN GVIA
 0.1mg, 0.5mg & 1.0mg
08CON002
ω-Conotoxin MVIIC
 0.1mg, 0.5mg & 1.0mg
08SNX001
SNX482
 0.05mg & 0.1mg
 
* 다른 사이즈나 bulk 공급도 가능하오니 별도로 문의하여 주십시오.
 
 
Maurocalcine / Huwentoxin I / ω CONOTOXIN SO-3/Omega contoxin SO-3 / ω-Conotoxin MVIIA/Omega conotoxin MVIIA
 
 
▣ 관련 페이지 ; Smartox Biotechnology
 
• 화학 합성의 각종 TRP Channel Blocker Peptide Toxin
  GsMTx4 / Vanillotoxin-3 (VaTx3)
 
• 화학 합성의 각종 ASIC Channel Blocker Peptide Toxin
  Psalmotoxin-1 (PcTx1, Pi-theraphotoxin-Pc1a) / APETx2
 
• 화학 합성의 각종 Chloride Channel Blocker Peptide Toxin
  GaTx1 / GaTx2 / Chlorotoxin
 
• 화학 합성의 각종 Calcium Channel Blocker Peptide Toxin
  ω-agatoxin IVA / ω-CONOTOXIN GVIA/Omega conotoxin GVIA / ω-Conotoxin MVIIC/Omega conotoxin MVIIC /
  SNX482/ Maurocalcine/Huwentoxin I/ω CONOTOXIN SO-3/Omega contoxin SO-3/ω-Conotoxin MVIIA/
  Omega conotoxin MVIIA
 
• 화학 합성의 각종 Potassium Channel Blocker Peptide Toxin
  Iberiotoxin (IbTx) / Charybdotoxin / Leiurotoxin 1 / Tamapin / Guangxitoxin 1E / ShK (Stichodactyla toxin)/
  Margatoxin / HsTx1 / Apamin / TERTIAPIN-Q / Maurotoxin / Kaliotoxin-1
 
• 화학 합성의 각종 Sodium Channel Blocker Peptide Toxin
  Protoxin I (ProTx-1) / GsAF-I / GsAF-II / Jingzhaotoxin III / Biotinyl-Protoxin II (ProTx II) /  Hainantoxin-IV /
  Protoxin II (ProTx II) / Huwentoxin IV / Huwentoxin I / μ Conotoxin PIIIA / mu conotoxin PIIIA