|Product Name||Cat #||Size|
|APC-010||1 x 0.2 ml|
Anti-KV1.2 (extracellular) Antibody
|APC-162||1 x 0.2 ml|
|D-400||1 x 70 µg|
KV1.2 Channel Overexpressed Membrane Fractions Antibody
|LX-101||2 x 0.1 ml|
|STT-360||1 x 10 µg|
- Lyophilized Powder Lyophilized Powder
This product is freeze dried. All water molecules have been removed.
- Antigen Incl. Control Antigen Included
This antibody is shipped with its antigen FREE of charge!
- Bioassay Tested Bioassay Tested
This antibody has undergone quality control and has been approved by our professional team.
- QC Tested QC Tested
The activity of this product has been verified and approved by our professional team.
- Shipped at Room Temp. Shipped at Room Temp.
This lyophilized product is shipped at room temperature. Please see its certificate of analysis for further storage instructions.
- Live Cell Imaging Live Cell Imaging
This product has been tested in living cells.
- 100% Net Peptide 100% Net Peptide
This vial contains 100% net peptide content.
Alomone Labs is pleased to offer the KV1.2 Channel Basic Research Pack (#ESB-500). The Research Pack contains all you need for KV1.2 research: Antibodies recognizing different domains of the channel, membrane lysates expressing KV1.2 channel- your ideal control for western blot analysis and specific KV1.2 blockers, all in one economical package!
KV1.2 is a mammalian voltage dependent K+ channel, homologous to the Drosophila Shaker K+ channel. KV1.2 was first cloned from rat brain.1 Eight Shaker related genes exist in mammals constituting the KV1, subfamily of the large KV channel family of genes.2
A functional KV1 channel is either a membrane spanning homotetramer or heterotetramer, which is composed of members of the same subfamily. In addition several auxiliary subunits and intracellular proteins might interact with the channel and affect its function.
The structure of KV1.2 channel is similar to all KV channels and includes six membrane spanning helixes creating a voltage sensor domain and a pore domain. 2
The channel is expressed in neurons and cardiac and smooth muscle tissue as well as in retina and pancreas.2 The crystal structure of KV1.2 was recently solved shading light on the structure of a mammalian voltage dependent channel.3 The functional channel is considered low voltage activated and shows very little inactivation. Therefore, this channel activity influences the membrane potential and excitability of neurons and muscle.
KV1.2 channels are sensitive to high doses of TEA (560 mM) and low doses of 4-AP (0.59 mM), the “classical” non-selective potassium channel blockers.
Several venomous toxins from Snakes, Scorpions and Honey Bee are potent blockers (affecting the channels in the nanomolar range) of KV1.2 channels. Among these the most potent and selective are α-Dendrotoxin (#D-350, 1-12 nM), Dendrotoxin-I (#D-390, 0.13 nM), Maurotoxin (#STM-340, 0.1-0.8 nM), Hongotoxin-1 (#RTH-400, 0.17 nM), Margatoxin (#STM-325, 0.16-0.65 nM), Tityustoxin Kα (#STT-360, 0.21 nM) and MCD peptide (#STM-250, 10-400 nM).4