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Merck
CN

M7444

Sigma-Aldrich

Maurotoxin

recombinant, expressed in E. coli, ≥95% (HPLC), lyophilized powder

别名:

MTX scorpion toxin

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关于此项目

MDL编号:
UNSPSC代码:
12352200
NACRES:
NA.77
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重组

expressed in E. coli

质量水平

方案

≥95% (HPLC)

表单

lyophilized powder

分子量

3613

运输

wet ice

储存温度

−20°C

Amino Acid Sequence

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

生化/生理作用

Maurotoxin is a 34 amino acid recombinant toxin, originally isolated from the venom of the scorpion Scorpio Maurus palmatus; 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).
Scorpion toxin that blocks voltage-gated potassium channels KV1.1, KV1.2, and KV1.3, and inhibits SK channels, particularly KCa3.1(IKca1, SK4).

特点和优势

This compound is featured on the Potassium Channels page of the Handbook of Receptor Classification and Signal Transduction. To browse other handbook pages, click here.

制备说明

Stock solution of 1 μm can be obtained by adding 0.277 mL of any conventional buffer per μg of protein.

储存分类代码

11 - Combustible Solids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, type N95 (US)

法规信息

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分析证书(COA)

Lot/Batch Number

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N A Castle et al.
Molecular pharmacology, 63(2), 409-418 (2003-01-16)
Maurotoxin, a 34-amino acid toxin from Scorpio maurus scorpion venom, was examined for its ability to inhibit cloned human SK (SK1, SK2, and SK3), IK1, and Slo1 calcium-activated potassium (K(Ca)) channels. Maurotoxin was found to produce a potent inhibition of
Violeta Visan et al.
Molecular pharmacology, 66(5), 1103-1112 (2004-08-03)
Maurotoxin (MTX) is a potent blocker of human voltage-activated Kv1.2 and intermediate-conductance calcium-activated potassium channels, hIKCa1. Because its blocking affinity on both channels is similar, although the pore region of these channels show only few conserved amino acids, we aimed
Ricardo C Rodríguez de la Vega et al.
Toxicon : official journal of the International Society on Toxinology, 43(8), 865-875 (2004-06-23)
Much of our knowledge on K+-channels was elucidated using specific peptide ligands isolated from a number of venomous organisms. Recently, this field received a strong support and increased interest due to the solution of the three-dimensional structure of a couple

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