화학합성의 Calcium Channel Blocker Peptide Toxin(1)
본문
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
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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
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
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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) |
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Length (aa): |
|
27 |
|
Formula: |
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C120H182N38O43S6 |
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Molecular Weight: |
|
3036.05 Da |
|
Appearance: |
|
White lyophilized solid |
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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
2. Seiji Ichida, et al. (2005) Characteristics of Omega-conotoxin GVIA and MVIIC Binding to Cav 2.1 and Cav 2.2
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
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
2. Bourinet, E., et al. (2001) Interaction of SNX482 with domains III and IV inhibits activation gating of alpha(1E)
3. Newcomb, R., et al. (1998) Selective peptide antagonist of the class E calcium channel from the venom of the
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
- 이전글화학합성의 Calcium Channel Blocker Peptide Toxin(2) 13.05.29
- 다음글화학합성의 Potassium Channel Blocker Peptide Toxin(2) 13.05.16
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