Kv1 Assays
What is Kv1 Channel?
The potassium channel is a channel that selectively allows potassium ions to pass through the cell membrane and hinders the passage of other ions, especially sodium ions. The potassium channel generally consists of 4 major classes: voltage-gated potassium channel, calcium/sodium activated potassium channel, inwardly rectifying potassium channel, and two P domain potassium channels. Voltage-gated potassium (Kv) channel is a large family of potassium channels with 12 subfamilies (about 40 members) have been identified, in which Kv1 is one of the most important subfamilies playing key roles in neural excitability regulation.
Structure of Kv1 Channel
Kv1 channel is composed of pore-forming α subunits and β subunits, where the pore-forming α subunits are structures with six hydrophobic transmembrane domains (S1-S6) and a P-domain, and β subunits are auxiliary proteins that associate with α subunits and affect the properties of the channels. The N-terminus of the α subunit is connected with the β subunit, which affects the expression and inactivation properties of the channel. The C-terminus of the α subunit is associated with the PDZ domain protein responsible for channel targeting.
The Kv1 channel proteins usually are expressed in a heteromeric form as well as in a homologous assembly of the four Kv1α subunits. This different assembly of α subunits and location in different cellular compartments are the main causes of diverse bio functions of Kv1 channels.
Fig.1 Schematic representation of a Kv subunit. (Rudy, 2009)
Subtypes and Functions of Kv1 Channels
8 members have been identified in the Kv1 channel family, Kv1.2, Kv1.3, Kv1.4, Kv1.5, Kv1.6, Kv1.7, and Kv1.8, all of which are important voltage-gated potassium channels contributing to transmembrane potassium transport and membrane potential regulation.
| Subtype | Gene | Pathways | Function |
| Kv1.1 | KCNA1 |
|
Regulates the membrane potential or voltage, a regulator of neuronal excitability. |
| Kv1.2 | KCNA2 |
|
Regulates the membrane potential or voltage, and prevents aberrant action potential firing. |
| Kv1.3 | KCNA3 |
|
Regulates membrane potential of T cell, and has a key role in T cell proliferation and activation. |
| Kv1.4 | KCNA4 |
|
Regulates the cardiac transient outward potassium current. |
| Kv1.5 | KCNA5 |
|
Restores the resting membrane potential of beta cells thereby regulating insulin secretion. |
| Kv1.6 | KCNA6 |
|
Mediates transmembrane potassium transport in excitable membranes. |
| Kv1.7 | KCNA7 |
|
Regulates the cardiac transient outward potassium current. |
| Kv1.8 | KCNA10 |
|
Mediates voltage-dependent potassium ion permeability of excitable membranes. |
Assay List of Kv1 Channel
Creative Biolabs can provide a range of assays of Kv1 channels. You can choose the assay in the list or contact us for more information:
Published Data
| Paper Title | Disruption of Kv1.3 Channel Forward Vesicular Trafficking by Hypoxia in Human T Lymphocytes |
| Journal | Journal of Biological Chemistry |
| Published | 2012 |
| Abstract | Hypoxia inducing reduced immunosurveillance has been reported associated with the down-regulation of Kv1.3 channels in T lymphocytes. Here, various assays have been formed to figure out the mechanisms responsible for Kv1.3 down-regulation. |
| Result |
The results of immunofluorescence, confocal microscopy, and other characterization assays indicated that hypoxia could result in increased retention of Kv1.3 in the trans-Golgi, and reduced expression of adaptor protein-1. And, down-expression of adaptor protein-1 also had similar functions, which decreased the Kv1.3 current amplitude and Kv1.3 surface expression in T lymphocytes.
|
Fig.2. Down-regulation of AP1 mimics the effect of hypoxia on Kv1.3 surface expression. (Chimote, 2012)
References
- Rudy, B.; et al. Voltage Gated Potassium Channels: Structure and Function of Kv1 to Kv9 Subfamilies. In Encyclopedia of Neuroscience. 2009, pp: 397-425, https://doi.org/10.1016/B978-008045046-9.01630-2.
- Chimote, A.A.; et al. Disruption of Kv1.3 Channel Forward Vesicular Trafficking by Hypoxia in Human T Lymphocytes. Journal of Biological Chemistry. 2012, 287(3): 2055-2067.
