Kv1 Related Drug Discovery Products
Membrane protein stable cell lines are widely used in many areas of biomedical research. Creative Biolabs can offer membrane protein stable cell lines to stablish in vitro models for High Throughput Screening.
Creative Biolabs offers high-quality, innovative tools to help research groups accelerate membrane protein drug discovery. They can be found by targets. If there is no product that meets your needs, please contact us.
One of the first ion channels to be discovered was voltage-gated. Kv1 channels are present in the CNS neurons' axons and synaptic terminals as well as in the juxtaparanodal sections of myelinated axons in both the CNS and PNS. These channels aid in the regulation of action potential propagation and neurotransmitter release in the mammalian nervous system. Some CNS neurons' somatodendritic areas also contain Kv1 channels. The exocytic machinery in presynaptic terminals and a contactin-associated protein-2 (CASPR2)-TAG1-4.1B complex in the juxtaparanodal areas are two examples of other proteins that Kv1 subunits bind with or colocalize with. The interacting proteins and motifs that are important in axonal targeting, channel trafficking, and the clustering of these channels have been investigated, even though a precise targeting mechanism for Kv channels has not yet been identified.
Creative Biolabs offers a range of Kv1 assays and products with our high-efficient drug discovery strategy in a timely and cost-effective manner:
Overview of Kv1
Axonal targeting, which most likely involves mechanisms other than preferential endocytosis from dendrites, is likewise dependent on the N-terminal T1 domain of Kv1 α-subunits; directed targeting may be involved, although this may depend on the kind of neuron. The most prevalent -subunits in the brain, Kv1.1, Kv1.2, and Kv1.4, can interact with Kvβ1 and Kvβ2 subunits through the T1 domain. Kvβ subunits have been linked to encouraging the surface expression and axonal targeting of Kv1 channels. They share similarities with aldo-keto reductase enzymes in their protein fold or structure and in their capacity to bind the NADP+ moiety. The intriguing question of whether the cell's redox state could control Kv1 axonal targeting is raised by the observation that mutations that change the NADP+ binding site but not those that affect the putative catalytic active site have an impact on axonal targeting. T1 mutations that influence axonal targeting do not always affect Kvβ binding, suggesting that minute structural variations in the T1-Kvβ interaction can have an impact on axonal targeting.
Kv1 Drug Discovery
The development of drugs for ion channels has generally trailed behind that of G protein-coupled receptors and protein kinases due to the challenges of targeting ion channels in general. The same general issues that plague target fields across the board, including the potential for target evaluation to be misled by transgenic techniques, are present in KV channel drug research. There are a variety of potential causes for this, from developmental compensation to the various physiological functions of certain KV channels in various species. Our understanding of how pharmaceuticals target K+ channels has been transformed by the X-ray structures of K+ channels in the open and closed states. More and more scientists are employing homology modeling and ligand docking to understand the results of mutational, electrophysiological, and ligand-binding research in structural terms.
