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  • 產品名稱：rBmP05K+channeltoxin-KTx5.3

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  • 產品廠商：BioLeaf
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簡單介紹：
rBmP05K+channeltoxin-KTx5.3
詳情介紹：
Sequence AVCNLKRCQL SCRSLGLLGK CIGDKCECVK H.
Specificity BmP05 blocks SKCa2 and SKCa3 channels with IC50 of 0.09 nM and 0.13 nM channels respectively.
Characteristics Source: Mesobuthus Martensii (Buthus martensii)
Molecular formula: C139H239N45O40S6.
Disulfide bonds between Cys3-Cys21, Cys8-Cys26, and Cys12-Cys28.
Purity > 98 %
Background BmP05 inhibits SKCa3 channels heterologously expressed in HEK-293 cells. SKCa3 channel currents, before and after application of 100nM rBmP05. The SKCa currents were elicited by 1μM internal calcium and 200 ms voltage ramps from -140 to +40 mV at the holding potential of 0 mV.
Molecular Weight 3372
Application Notes 0.1-10nM
Restrictions For Research Use only
Format Lyophilized
Reconstitution Any aqueous buffer. Centrifuge all product preparations before use (10000 x g 5 min).
Concentration after reconstitution: Dissolving 50g in 1.483ml will provide a stock solution of 10 M.
Handling Advice Soluble in Water.
Supplier Images
image for rBmP05K+ channel toxin -KTx 5.3 (ABIN1001636) SKCa3 channel currents, before and after application of 100nM rBmP05. The SKCa curren...
Product cited in: Wu, He, Zhou, Chi: "Gene expression, mutation, and structure-function relationship of scorpion toxin BmP05 active on SK(Ca) channels." in: Biochemistry, Vol. 41, Issue 8, pp. 2844-9, 2002 (PubMed).

Xu, Wu, Pei, Shi, Ji, Tong: "Solution structure of BmP02, a new potassium channel blocker from the venom of the Chinese scorpion Buthus martensi Karsch." in: Biochemistry, Vol. 39, Issue 45, pp. 13669-75, 2000 (PubMed).

Wu, Dai, Lan, Chi: "Genomic organization of three neurotoxins active on small conductance Ca2+-activated potassium channels from the scorpion Buthus martensi Karsch." in: FEBS letters, Vol. 452, Issue 3, pp. 360-4, 1999 (PubMed).

Romi-Lebrun, Martin-Eauclaire, Escoubas, Wu, Lebrun, Hisada, Nakajima: "Characterization of four toxins from Buthus martensi scorpion venom, which act on apamin-sensitive Ca2+-activated K+ channels." in: European journal of biochemistry / FEBS, Vol. 245, Issue 2, pp. 457-64, 1997 (PubMed).

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