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Merck
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重要文件

M7444

Sigma-Aldrich

Maurotoxin

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

同義詞:

MTX scorpion toxin

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About This Item

MDL號碼:
分類程式碼代碼:
12352200
NACRES:
NA.77

重組細胞

expressed in E. coli

品質等級

化驗

≥95% (HPLC)

形狀

lyophilized powder

分子量

3613

運輸包裝

wet ice

儲存溫度

−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).

特點和優勢

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.

重構

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

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

Eyeshields, Gloves, type N95 (US)


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分析證明 (COA)

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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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