Antigen: fusion protein amino acids 437-585 of rat Kv3.1b · Clone designation: S16B-8 · Host: Mouse · Isotype: IgG₁ · Application(s): IHC and WB · Ion channels are integral membrane proteins that help establish and control the small voltage gradient across the plasma membrane of living cells by allowing the flow of ions down their electrochemical gradient.¹ They are present in the membranes that surround all biological cells and their main function is to regulate the flow of ions across this membrane. Whereas some ion channels permit the passage of ions based on charge, others conduct based on a ionic species, such as sodium or potassium. Furthermore, in some ion channels, the passage is governed by a gate which is controlled by chemical or electrical signals, temperature, or mechanical forces. There are a few main classifications of gated ion channels. There are voltage-gated ion channels, ligand-gated, other gating systems, and finally those that are classified differently, having more exotic characteristics. The first are voltage-gated ion channels which open and close in response to membrane potential. These are then seperated into sodium, calcium, potassium, proton, transient receptor, and cyclic nucleotide-gated channels, each of which is responsible for a unique role. Ligand-gated ion channels are also known as ionotropic receptors and they open in response to specific ligand molecules binding to the extracellular domain of the receptor protein. The other gated classifications include activation and inactivation by second messengers, inward-rectifier potassium channels, calcium-activated potassium channels, two-pore-domain potassium channels, light-gated channels, mechano-sensitive ion channels, and cyclic nucleotide-gated channels. Finally, the other classifications are based on less normal characteristics such as two-pore channels and transient receptor potential channels.² Potassium voltage-gated channel, Shaw-related subfamily, member 1, also known as KCNC1 or Kv3.1, is a human gene. The Shaker gene family of Drosophila encodes components of voltage-gated potassium channels and is comprised of four subfamilies. Based in sequence similarity, this gene is similar to one of these subfamilies, namely the Shaw subfamily.³ The protein encoded by this gene belongs to the delayed rectifier class of channel proteins and is an integral membrane protein that mediates the voltage-dependent potassium ion permeability of excitable membranes. Kv3.1b has been extensively tested in the auditory regions of mammals, and the decline of Kv3.1b expression appears to correlate with the functional decline in the medial olivocochlear efferent system.⁴ Other research shows potential for Kv3.1b channels to be oxygen sensors.⁵

1 Hille, B. Ion Channels of Excitable Membranes. 3rd (2001).

2 . What are ion channels? (2004).

3 Xu, M., Cao, R., Xiao, R., et al. The axon-dendrite targeting of Kv3 (Shaw) channel is determined by a targeting motif that associates with the T1 domain and ankyrin G. J Neurosci 27(51) 14158-14170 (2007).

4 Zettel, M.L., Zhu, X., O'Neill, W.E., et al. Age-related decline in Kv3.1b expression in the mouse auditory brainstem correlates with functional deficits in the medial olivocochlear efferent system. J Assoc Res Otolaryngol 8 280-293 (2007).

5 Osipenko, O.N., Tate, R.J., and Gurney, A.M. Potential role for Kv3.1b channels as oxygen sensors. Circ Res 86 534-540 (2000).

Hille, B. Ion Channels of Excitable Membranes. 3rd (2001).

. What are ion channels? (2004).

Zettel, M.L., Zhu, X., O'Neill, W.E., et al. Age-related decline in Kv3.1b expression in the mouse auditory brainstem correlates with functional deficits in the medial olivocochlear efferent system. J Assoc Res Otolaryngol 8 280-293 (2007).

Xu, M., Cao, R., Xiao, R., et al. The axon-dendrite targeting of Kv3 (Shaw) channel is determined by a targeting motif that associates with the T1 domain and ankyrin G. J Neurosci 27(51) 14158-14170 (2007).

Osipenko, O.N., Tate, R.J., and Gurney, A.M. Potential role for Kv3.1b channels as oxygen sensors. Circ Res 86 534-540 (2000).

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