Overview
Lyophilized Powder yes
Origin Natural peptide isolated from Dendroaspis angusticeps (Eastern green mamba).
MW: ~7000 Da
Purity: >98% (HPLC)
Effective concentration 10-500 nM.
Activity β-Dendrotoxin inhibits 4-AP sensitive, inactivating voltage-gated K+ channels (KV1.1, KV1.2).
Shipping and storage Shipped at room temperature. Product as supplied can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.
Solubility Any aqueous buffer. Centrifuge all product preparations before use (10000 x g 5 min).
Storage of solutions Up to four weeks at 4°C or three months at -20°C.
Our bioassay
Alomone Labs β-Dendrotoxin inhibits cloned KV1.1 and KV1.2 channel currents heterologously expressed in Xenopus oocytes.KV1.1 (left, in 2 mM K+) and KV1.2 (right, in 5 mM K+) channel currents, elicited by 200 ms depolarization from holding potential of -100 mV to +20 mV, before and during application of 100 nM β-Dendrotoxin (#D-360). 62% (n = 4) of the KV1.1 and 74% (n = 4) of the KV1.2 channels were inhibited by 100 nM β-Dendrotoxin, respectively.
References - Scientific background
- Benishin, C.G. et al. (1988) Mol. Pharmacol. 34, 152.
- Harvey, A.L. and Anderson, A.J. (1985) Pharmacol. Ther. 31, 33.
Scientific background β-Dendrotoxin is found in the Dendroaspis angusticeps snake venom1,2. It blocks KV1.1 and KV1.2 channels expressed in Xenopus oocytes.
Target KV1.1, KV1.2 K+ channels
Peptide Content: 100%
Lyophilized Powder
β-Dendrotoxin (#D-360) is a highly pure, natural, and biologically active peptide toxin.
For research purposes only, not for human use
Last Update: 02/01/2024
Applications
Citations
Citations
Powered by BiozProduct citations
- Manicam, C. et al. (2017) Sci. Rep. 7, 7111.
- Manicam, C. et al. (2016) Sci. Rep. 6, 20322.
- Tang, G. and Wang, R. (2001) Pflugers Arch. 442, 124.
- Hirschberg, B. et al. (1999) Biophys. J. 77, 1905.
- Zygmunt, P.M. et al. (1997) Br. J. Pharmacol. 121, 141.
