Smartox Biotechnology
 
작성일 : 13-05-16
[Smartox Biotechnology] 화학합성의 Potassium Channel Blocker Peptide Toxin(2)
Margatoxin / HsTx1 / Apamin / TERTIAPIN-Q / Maurotoxin / Kaliotoxin-1
 
화학합성의 각종 Potassium Channel Blocker Peptide Toxin (2)
 
Potassium channel 연구에 유용한 유독 생물 유래의 합성 peptide toxin 입니다. 화학합성 peptide이기 때문에
endotoxin 오염의 걱정이 없습니다.
 
 
Margatoxin
 
Margatoxin is a component of the venom of Scorpio Centruroides margaritatus. This toxin is a potent selective inhibitor of
voltage-dependent potassium channels such as Kv1.3.
 
Details
AA sequence:
 
H-Thr-Ile-Ile-Asn-Val-Lys-Cys7-Thr-Ser-Pro-Lys-Gln-Cys13-Leu-Pro-Pro-Cys17-Lys-Ala-Gln-Phe-
Gly-Gln-Ser-Ala-Gly-Ala-Lys-Cys29-Met-Asn-Gly-Lys-Cys34-Lys-Cys36-Tyr-Pro-His-OH
 
 
(Disulfide bonds between Cys7-Cys29, Cys13-Cys34 and Cys17-Cys36)
Length (aa):
 
39
Formula:
C178H286N52O50S7
Molecular Weight:
 
4179.03 Da
Appearance:
 
White lyophilized solid
Solubility:
 
Water and saline buffer
CAS number:
145808-47-5
Source:
 
Synthetic
Purity rate:
 
> 97 %
 
References
1. Bednarek, M. A., et al. (1994) Chemical synthesis and structure-function studies of margatoxin, a potent inhibitor
   of voltage-dependent potassium channel in human T lymphocytes, Biochem Biophys Res Commun.
2. Garcia-Calvo, et al. (1993) Purification, characterization, and biosynthesis of margatoxin, a component of
   Centruroides margaritatus venom that selectively inhibits voltage-dependent potassium channels, J Biol Chem.
3. Johnson, B. A., et al. (1994) Determination of the three-dimensional structure of margatoxin by 1H, 13C, 15N triple-
   resonance nuclear magnetic resonance spectroscopy, Biochemistry.
 
 
HsTx1
 
HsTx1 is a member of the a-KTx6 family of scorpion toxins active on voltage-gated K+v1.3 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. It is
one of the most potent toxins active on K
 
Details
AA sequence:
 
H-Ala-Ser-Cys3-Arg-Thr-Pro-Lys-Asp-Cys9-Ala-Asp-Pro-Cys13-Arg-Lys-Glu-Thr-Gly-Cys19-Pro-
Tyr-Gly-Lys-Cys24-Met-Asn-Arg-Lys-Cys29-Lys-Cys31-Asn-Arg-Cys34-NH2
 
 
(Disulfide bonds between Cys3-Cys24, Cys9-Cys29 , Cys13-Cys31and Cys19-Cys34 )
Length (aa):
 
34
Formula:
C149H246N54O46S9
Molecular Weight:
 
3819.87 Da
Appearance:
 
White lyophilized solid
Solubility:
 
Water and saline buffer
CAS number:
Not available
Source:
 
Synthetic
Purity rate:
 
> 95 %
 
References
1. Savarin, P., et al. (1999) Structural and functional consequences of the presence of a fourth disulfide
   bridge in the scorpion short toxins: solution structure of the potassium channel inhibitor HsTX1.
   Protein Sci. PubMed link
2. Lebrun, B., et al. (1997) A four-disulphide-bridged toxin, with high affinity towards voltage-gated K+
   channels, isolated from Heterometrusspinnifer (Scorpionidae) venom. Biochem. PubMed link
 
 
Apamin
 
Apamin is a neurotoxin that was originally isolated from Apis mellifera. Apamin binds to and inhibits the SK channels (small
conductance Ca2+-activated K+ channels) in the brain and spinal cord. It inhibits three subtypes of SK channels (SK1,
SK2, and SK3) with different affinity. Apamin most likely acts as a pore blocker, although residues both inside and outside
of the pore region of the SK channels participate in0 apamin binding. The SK channels are present in a wide range of
excitable and non-excitable cells, including cells in the central nervous system, intestinal myocytes, endothelial cells, and
hepatocytes.
 
Details
AA sequence:
 
H-Cys1-Asn-Cys3-Lys-Ala-Pro-Glu-Thr-Ala-Leu-Cys11-Ala-Arg-Arg-Cys15-Gln-Gln-His-NH2
 
 
(Disulfide bonds between Cys1-Cys11 and Cys3-Cys15 )
Length (aa):
 
18
Formula:
C79H131N31O24S4
Molecular Weight:
 
2027.34 Da
Appearance:
 
White lyophilized solid
Solubility:
 
Water and saline buffer
CAS number:
24345-16-2
Source:
 
Synthetic
Purity rate:
 
> 98 %
 
References
1. Habermann E (1984). Apamin. Pharmacol Ther. PubMed Link
2. Strong PN (1990). Potassium channel toxins. Pharmacol Ther. PubMed link
3. Castle NA. et al. (1989). Toxins in the characterization of potassium channels. Trends Neurosci. PubMed link
 
 
TERTIAPIN-Q
 
Tertiapin has been isolated from the venom of the Honeybee Apis mellifera (African tarantula) tertiapin-Q is a mutant of
tertiapin where M13 has been mutated by Q in order to increase your stability. This is a 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-
dependent acetylcholine(ACh)-induced atrioventricular blocks in mammalian hearts, as KCNJ3/KCNJ5 channels (also named
I(KACh)), are activated by ACh found in mammalian myocytes. This toxin interacts specifically with calmodulin in the
presence of calcium.
 
Details
AA sequence:
 
H-Ala-Leu-Cys3-Asn-Cys5-Asn-Arg-Ile-Ile-Ile-Pro-His-Gln-Cys14-Trp-Lys-Lys-Cys18-Gly-Lys-Lys-
NH2
 
(Disulfide bonds between Cys3-Cys14 and Cys5-Cys18)
Length (aa):
 
21
Formula:
C106H175N35O24S4
Molecular Weight:
 
2453.39 Da
Appearance:
 
 White lyophilized solid
Solubility:
 
Water and saline buffer
CAS number:
252198-49-5
Source:
 
Synthetic
Purity rate:
 
> 97 %
 
References
1. Felix, J. P.,et al. (2006) Characterization of Kir1.1 channels with the use of a radiolabeled derivative of tertiapin,
   Biochemistry. PubMed link
2. Kanjhan, R., C et al. (2005) Tertiapin-Q blocks recombinant and native large conductance K+ channels in a
   use-dependent manner, J Pharmacol Exp Ther. PubMed link
3. Ramu, Y., et al. (2001) Titration of tertiapin-Q inhibition of ROMK1 channels by extracellular protons, Biochemistry.
4. Kitamura, H., et al. (2000) Tertiapin potently and selectively blocks muscarinic K(+) channels in rabbit cardiac
   myocytes, J Pharmacol Exp Ther. PubMed link
5. Jin, W., et al. (1999) Mechanisms of inward-rectifier K+ channel inhibition by tertiapin-Q, Biochemistry. PubMed link
6. Jin, W., and Lu, Z. (1999) Synthesis of a stable form of tertiapin: a high-affinity inhibitor for inward-rectifier
   K+ channels, Biochemistry. PubMed link
 
 
Maurotoxin
 
Maurotoxin is a component of the venom of Scorpio maurus palmatus.This toxin is a member of the α-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).
The blockage of Kv1.2 occurs with high affinity.
 
Details
AA sequence:
 
H-Val-Ser-Cys3-Thr-Gly-Ser-Lys-Asp-Cys9-Tyr-Ala-Pro-Cys13-Arg-Lys-Gln-Thr-Gly-Cys19-Pro-
Asn-Ala-Lys-Cys24-Ile-Asn-Lys-Ser-Cys29-Lys-Cys31-Tyr-Gly-Cys34-NH2
 
 
(Disulfide bonds between Cys3-Cys24, Cys9-Cys29, Cys13-Cys19 and Cys31-Cys34 )
Length (aa):
 
34
Formula:
C145H231N45O47S8
Molecular Weight:
 
3612.55 Da
Appearance:
 
White lyophilized solid
Solubility:
 
Water and saline buffer
CAS number:
Not available
Source:
 
Synthetic
Purity rate:
 
> 95 %
 
References
1. Fajloun Z, et al., (2011) Analysis of the interacting surface of maurotoxin with the voltage-gated Shaker B K(+)
   channel. J Pept Sci. PubMed link
2. Carlier, E.,et al. (2000) Effect of maurotoxin, a four disulfide-bridged toxin from the chactoid scorpion Scorpio maurus,
   on Shaker K+ channels, J Pept. PubMed link
3. Rochat, H., et al. (1998) Maurotoxin, a four disulfide bridges scorpion toxin acting on K+ channels,
   Toxicon. PubMed link
4. Blanc, E., et al. (1997) Solution structure of maurotoxin, a scorpion toxin from Scorpio maurus, with high affinity for
   voltage-gated potassium channels, Proteins. PubMed link
 
 
Kaliotoxin-1
 
Kaliotoxin-1 (KTX1) has been isolated from the venom of the Scorpion Androctonus mauretanicus mauretanicus. KTX1
shows a high structural affinty with Iberiotoxin and charybdotoxin that inhibit KCa channels activity. According to several
studies, it appears that KTX1 has a weak inhibitory effect on KCa channels, but it is a potent and selective inhibitor of
voltage-activated potassium channel (Kv1.1, Kv1.2, Kv1.3).
 
Details
AA sequence:
 
Gly-Val-Glu-Ile-Asn-Val-Lys-Cys8-Ser-Gly-Ser-Pro-Gln-Cys14-Leu-Lys-Pro-Cys18-Lys-Asp-Ala-Gly-Met-Arg-Phe-Gly-Lys-Cys28-Met-Asn-Arg-Lys-Cys33-His-Cys35-Thr-Pro-Lys-OH
 
(Disulfide bonds between Cys8-Cys28, Cys14-Cys33 and Cys18-Cys35 )
Length (aa):
 
38
Formula:
C171H283N55O49S6
Molecular Weight:
 
4149.89 Da
Appearance:
 
 White lyophilized solid
Solubility:
 
Water and saline buffer
CAS number:
Not available
Source:
 
Synthetic
Purity rate:
 
> 97 %
 
References
1. Mourre C, et al. Distribution in rat brain of binding sites of kaliotoxin, a blocker of Kv1.1 and Kv1.3 alpha-subunits.
   J Pharmacol Exp Ther.
2. Gairí M, et al. 3D structure of kaliotoxin: is residue 34 a key for channel selectivity? J Pept Sci.
3. Rader RK, et al. T cell activation is regulated by voltage-dependent and calcium-activated potassium channels.
   J Immunol.
4. Gribkoff VK. Effects of channel modulators on cloned large-conductance calcium-activated potassium channels.
    Mol Pharmacol.
5. Eder C. Pharmacological properties of Ca2+activated K+ currents of ramified murine brain macrophages.
   Naunyn Schmiedebergs Arch Pharmacol.
 
 
Ordering informations
 
Catalog No.
Product Name
Size
08MAG001
Margatoxin
 0.1mg, 0.5mg & 1.0mg
08NEU001
HsTx1
 0.1mg
08APA001
Apamin
 0.5mg & 1.0mg
08TER001
TERTIAPIN-Q
 0.1mg, 0.5mg & 1.0mg
08MAR001
Maurotoxin
0.1mg, 0.5mg & 1.0mg
08KTX002
Kaliotoxin-1
0.1mg, 0.5mg & 1.0mg
 
* 다른 사이즈나 bulk 공급도 가능하오니 별도로 문의하여 주십시오.
 
 
* 관련 제품
 
Iberiotoxin (IbTx) / Charybdotoxin / Leiurotoxin 1 / Tamapin / Guangxitoxin 1E / ShK (Stichodactyla toxin)
 
 
▣ 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