화학합성의 Sodium Channel Blocker Peptide Toxin(2)
본문
화학합성의 각종 Sodium Channel Blocker Peptide Toxin (2)
Sodium channel 연구에 유용한 유독 생물 유래의 합성 peptide toxin 입니다. 화학합성 peptide이기 때문에
endotoxin 오염의 걱정이 없습니다.
Hainantoxin-IV
Hainantoxin-IV (HNTX-IV) is a peptide that was originally isolated from the venom of the Chinese bird spider
Ornithoctonus hainana Liang (Selenocosmia hainana Liang). It has been reported that this peptide is a potent antagonist
of tetrodotoxin-sensitive (TTX-S) voltage-gated sodium channels (VGSCs). It binds to TTX-S with an IC50value of 34 nM
in adult rat dorsal root ganglion (DRG) neurons. Tetrodotoxin-resistant (TTX-R) voltage-gated sodium channels are not
affected by hainantoxin IV. It probably interacts with the site 1 through a mechanism quite similar to that of TTX
without affecting the activation and inactivation kinetics.
Details
AA sequence: |
|
Glu-Cys2-Leu-Gly-Phe-Gly-Lys-Gly-Cys9-Asn-Pro-Ser-Asn-Asp-Gln-Cys16-Cys17-Lys-Ser-Ser-Asn-Leu-Val-Cys24-Ser-Arg-Lys-His-Arg-Trp-Cys31-Lys-Tyr-Glu-Ile-NH2 |
|
|
(Disulfide bonds between Cys2-Cys17, Cys9-Cys24, and Cys16-Cys31) |
Length (aa): |
|
35 |
Formula: |
|
C166H257N53O50S6 |
Molecular Weight: |
|
3987.6 Da |
Appearance: |
|
White lyophilized solid |
Solubility: |
|
Water and saline buffer |
CAS number: |
|
Not available |
Source: |
|
Synthetic |
Purity rate: |
|
> 97 % |
References
1. Dongling Li, et al. (2004) Structure-Activity Relationships of Hainantoxin-IV and Structure Determination of Active and
2. Liu Z, et al. (2003) Isolation and characterization of hainantoxin-IV, a novel antagonist of tetrodotoxin-sensitive sodium
channels from the Chinese bird spider Selenocosmia hainana, Cell Mol Life Sci. PubMed link
3. Liu Y, et al. (2012) A positively charged surface patch is important for hainantoxin-IV binding to voltage-gated sodium
channels. J Pept Sci. PubMed link
4, Wang W., et al. (2009) Determination of disulfide bridges of two spider toxins: Hainantoxin-III and Hainantoxin-IV. J
Venom Anim Toxins incl Trop Dis. PubMed link
Protoxin II (ProTx II)
Protoxin II (ProTx II) is a toxin that was originally isolated from Thrixopelma pruriens (Peruvian green velvet tarantula).
Protoxin II inhibits voltage-gated calcium and sodium channels (site 4). This toxin inhibits activation by shifting the
voltage-dependence of channel activation to more positive potentials. The toxin potently inhibits all sodium channel
subtypes tested (Nav1.2/SCN2A, Nav1.5/SCN5A, Nav1.7/SCN9A, and Nav1.8/SCN10A). It is approximately 15-fold more
potent on Nav1.7/SCN9A than on Nav1.5/SCN5A channels and 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. Protoxin
II also binds to phospholipids. ProTx-II, a selective inhibitor of Nav1.7 sodium channels, blocks action potential propagation
in nociceptors.
Details
AA sequence: |
|
Tyr-Cys2-Gln-Lys-Trp-Met-Trp-Thr-Cys9-Asp-Ser-Glu-Arg-Lys-Cys15-Cys16-Glu-Gly-Met-Val-
Cys21-Arg-Leu-Trp-Cys25-Lys-Lys-Lys-Leu-Trp-OH |
|
|
(Disulfide bonds between Cys2-Cys16, Cys9-Cys21 and Cys15-Cys25) |
Length (aa): |
|
30 |
Formula: |
|
C168H250N46O41S8 |
Molecular Weight: |
|
3828.00 Da |
Appearance: |
|
White lyophilized solid |
Solubility: |
|
Water or saline buffer |
CAS number: |
|
484598-36-9 |
Source: |
|
Synthetic |
Purity rate: |
|
> 95 % |
References
1. Edgerton G. B., et al. (2008) Evidence for multiple effects of ProTxII on activation gating in Na(V)1.5, Toxicon.
2. Priest B. T., et al. (2007) ProTx-I and ProTx-II: gating modifiers of voltage-gated sodium channels, Toxicon.
3. Smith J. J., et al. (2005) Differential phospholipid binding by site 3 and site 4 toxins. Implications for structural
variability between voltage-sensitive sodium channel domains, J Biol Chem. PubMed link
4. Middleton R. E., et al. (2002) Two tarantula peptides inhibit activation of multiple sodium channels, Biochemistry.
Huwentoxin IV
Huwentoxin IV is a neurotoxin that was originally isolated from Haplopelma schmidti (Chinese bird spider). This lethal
neurotoxin acts selectively on tetrodotoxin-sensitive (TTX-S) voltage-gated sodium channels, with an IC50 of 30 nM in rat
DRG neurons. It preferentially inhibits neuronal voltage-gated sodium channel subtype hNav1.7 (SCN9A) (IC50 is 26 nM),
rNav1.2 (SCN2A) (IC50 is 150 nM), and rNav1.3 (SCN3A) (IC50 is 338 nM), compared with muscle subtypes rNav1.4
(SCN4A) and hNav1.5 (SCN5A) (IC50 is > 10 µM). Huwentoxin IV inhibits the activation of sodium channels by trapping
the voltage sensor of domain II of the site 4 in the inward, closed configuration.
Details
AA sequence: |
|
H-Glu-Cys2-Leu-Glu-Ile-Phe-Lys-Ala-Cys9-Asn-Pro-Ser-Asn-Asp-Gln-Cys16-Cys17-Lys-Ser-Ser-
Lys-Leu-Val-Cys24-Ser-Arg-Lys-Thr-Arg-Trp-Cys31-Lys-Tyr-Gln-Ile-NH2 |
|
|
(Disulfide bonds between Cys2-Cys17, Cys9-Cys24 and Cys16-Cys31) |
Length (aa): |
|
35 |
Formula: |
|
C174H277N51O52S6 |
Molecular Weight: |
|
4109.18 Da |
Appearance: |
|
White lyophilized solid |
Solubility: |
|
Water or saline buffer |
CAS number: |
|
Not available |
Source: |
|
Synthetic |
Purity rate: |
|
> 97 % |
References
1. Xiao, Y., et al. (2011) Common molecular determinants of tarantula huwentoxin-IV inhibition of Na+ channel voltage
sensors in domains II and IV, JBC. PubMed link
2. Xiao, Y., et al. (2010) The tarantula toxins ProTx-II and huwentoxin-IV differentially interact with human Nav1.7
voltage sensors to inhibit channel activation and inactivation, Mol Pharmacol. PubMed link
3. Wang RL, et al. (2010) Mechanism of action of two insect toxins huwentoxin-III and hainantoxin-VI on voltage-gated
sodium channels. PubMed link
4. Xiao, Y., et al. (2008) Tarantula huwentoxin-IV inhibits neuronal sodium channels by binding to receptor site 4 and
trapping the domain ii voltage sensor in the closed configuration, JBC. PubMed link
5. Diao, J., et al. (2003) cDNA sequence analysis of seven peptide toxins from the spider Selenocosmia huwena,
Toxicon. PubMed link
6. Peng, K., et al. (2002) Function and solution structure of huwentoxin-IV, a potent neuronal tetrodotoxin (TTX)-
sensitive sodium channel antagonist from Chinese bird spider Selenocosmia huwena, J Biol Chem. PubMed link
Huwentoxin I
Huwentoxin I is a neurotoxin that was originally isolated from Haplopelma schmidti (Chinese bird spider) (Ornithoctonus
huwenum). This toxin selectively inhibits N-type calcium channels and has only a very weak effect on L-type calcium
channels. It has virtually no effect on muscle sodium channels but is a potent inhibitor of neuronal TTX-sensitive
channels, especially Nav1.7.
Details
AA sequence: |
|
H-Ala-Cys2-Lys-Gly-Val-Phe-Asp-Ala-Cys9-Thr-Pro-Gly-Lys-Asn-Glu-Cys16-Cys17-Pro-Asn-Arg-
Val-Cys22-Ser-Asp-Lys-His-Lys-Trp-Cys26-Lys-Trp-Lys-Leu-OH |
|
|
(Disulfide bonds between Cys2-Cys17, Cys9-Cys22 and Cys16-Cys29 ) |
Length (aa): |
|
33 |
Formula: |
|
C168H250N46O41S6 |
Molecular Weight: |
|
3751.77 Da |
Appearance: |
|
White lyophilized solid |
Solubility: |
|
Water or saline buffer |
CAS number: |
|
Not available |
Source: |
|
Synthetic |
Purity rate: |
|
> 97 % |
References
1. Wang M, et al. (2007) The cross channel activities of spider neurotoxin huwentoxin-I on rat dorsal root ganglion
neurons. Biochem Biophys Res Commun. PubMed link
2. Wang YR, et al. (2007) Effect of Huwentoxin-I on the Fas and TNF apoptosis pathway in the hippocampus of rat with
global cerebral ischemia. Toxicon. PubMed link
3. Peng, K., et al. (2001) The effect of Huwentoxin-I on Ca(2+) channels in differentiated NG108-15 cells, a patch-clamp
study, Toxicon. PubMed link
4. Liang, S. P., et al. (2000) The presynaptic activity of huwentoxin-I, a neurotoxin from the venom of the chinese bird
spider Selenocosmia huwena, Toxicon. PubMed link
5. Zhou, P. A., et al. (1997) Blockade of neuromuscular transmission by huwentoxin-I, purified from the venom of the
6. Liang, S. P., et al. (1993) Properties and amino acid sequence of huwentoxin-I, a neurotoxin purified from the venom
of the Chinese bird spider Selenocosmia huwena, Toxicon. PubMed link
μ Conotoxin PIIIA / mu conotoxin PIIIA
μ-Conotoxin PIIIA has been isolated from the venom of the cone Conus purpurascens. μ-Conotoxins bind and block site 1 of voltage-gated sodium channels. This toxin blocks the neuronal sodium channels Nav1.2 (SCN2A) and Nav1.7 (SCN9A).
The peptide causes flaccid paralysis in both mice and fish.
Details
AA sequence: |
|
H-pGlu-Arg-Leu-Cys4-Cys5-Gly-Phe-Hyp-Lys-Ser-Cys11-Arg-Ser-Arg-Gln-Cys16-Lys-Hyp-His-Arg-Cys21-Cys22-NH2 |
|
|
(Disulfide bonds between Cys4-Cys16, Cys5-Cys21 and Cys11-Cys22) |
Length (aa): |
|
22 |
Formula: |
|
C103H165N40O28S6 |
Molecular Weight: |
|
2604.10 Da |
Appearance: |
|
White lyophilized solid |
Solubility: |
|
water or saline buffer |
CAS number: |
|
Not available |
Source: |
|
Synthetic |
Purity rate: |
|
> 97 % |
References
1. Nielsen, K. J., et al. (2002) Solution structure of mu-conotoxin PIIIA, a preferential inhibitor of persistent tetrodotoxin-
sensitive sodium channels, J Biol Chem. PubMed link
2. Safo, P., et al. (2000) Distinction among neuronal subtypes of voltage-activated sodium channels by mu-conotoxin
PIIIA, J Neurosci. PubMed link
3. Shon, K. J., et al. (1998) mu-Conotoxin PIIIA, a new peptide for discriminating among tetrodotoxin-sensitive Na
channel subtypes, J Neurosci. PubMed link
Ordering informations
Catalog No. |
Product Name |
Size |
12HTX001 |
Hainantoxin-IV |
0.1mg, 0.5mg & 1.0mg |
07PTX002 |
ProTx II |
0.1mg, 0.5mg & 1.0mg |
08HWT002 |
Huwentoxin IV |
0.1mg, 0.5mg & 1.0mg |
07HWT001 |
Huwentoxin I |
0.1mg, 0.5mg & 1.0mg |
08CON006 |
μ-Conotoxin PIIIA |
0.1mg, 0.5mg & 1.0mg |
* 다른 사이즈나 bulk 공급도 가능하오니 별도로 문의하여 주십시오.
* 관련 제품
Protoxin I (ProTx-1) / GsAF-I / GsAF-II / Jingzhaotoxin III / Biotinyl-Protoxin II (ProTx II)
▣ 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
- 이전글Shield-1으로 단백질 발현을 제어할 수 있는 vector 13.05.14
- 다음글화학합성의 Sodium Channel Blocker Peptide Toxin(1) 13.05.10
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