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Merck

P222

Sigma-Aldrich

Pandinotoxin-Kα

>99%, powder

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About This Item

经验公式(希尔记法):
C169H267N53O48S7
分子量:
4033.71
MDL號碼:
分類程式碼代碼:
12352200
NACRES:
NA.32

化驗

>99%

形狀

powder

顏色

off-white

儲存溫度

−20°C

Amino Acid Sequence

Thr-Ile-Ser-Cys-Thr-Asn-Pro-Lys-Gln-Cys-Tyr-Pro-His-Cys-Lys-Lys-αGlu-Thr-Gly-Tyr-Pro-Asn-Ala-Lys-Cys-Met-Asn-Arg-Lys-Cys-Lys-Cys-Phe-Gly-Arg

一般說明

Pandinotoxin (PiTX)-Kα is a 35 amino acid peptide isolated from venom of the scorpion Pandinus imperaton. PiTX-Kβ and PiTXγ are other two members of pandinotoxin group. All the three pandinotoxins have structures similar to another scorpion toxin charybdotoxin (ChTX). The structure of PiTXs contains a β-sheet at the C- terminal end with three cysteines which is linked to the central α-helix by two disulfide bridges (C17-C35 and C13-C33) and to an extended amino-terminal fragment by the third disulfide bridge (C7-C28).

生化/生理作用

Pandinotoxin (PiTX) –Kα along with PiTX-Kβ and PiTXγ plays a vital role in blocking voltage-gated K+ channels.

法律資訊

Sold with the permission of University of Maryland.

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)


历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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D R Matteson et al.
The Journal of physiology, 503 ( Pt 2), 285-301 (1997-11-05)
1. The ability of three structurally homologous scorpion toxins to block voltage-dependent K+ currents in rat dorsal root ganglion neurones was examined using the patch-clamp technique. 2. Neurones with a diameter > 35 microns had two identifiable components of macroscopic
R S Rogowski et al.
Molecular pharmacology, 50(5), 1167-1177 (1996-11-01)
Three 35-amino acid peptide K+ channel toxins (pandinotoxins) were purified from the venom of the scorpion Pandinus imperaton the toxins are designated pandinotoxin (PiTX)-K alpha, PiTX-K beta, and PiTX-K gamma. In an 86Rb tracer flux assay on rat brain synaptosomes
T C Tenenholz et al.
Biochemistry, 36(10), 2763-2771 (1997-03-11)
PiTX-K alpha, a 35-residue peptide recently isolated from the venom of Pandinus imperator, blocks the rapidly inactivating (A-type) K+ channel(s) in rat brain synaptosomes and the cloned Kv 1.2 potassium channel at very low toxin concentrations (6 nM and 32

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