Voltage-gated potassium channel subunit beta-1 or Kvβ1.1 is encoded by the gene KCNAB1. Kvß1.1 is a member of the potassium channel, voltage-gated, shaker-related subfamily. Alternative splicing of KCNAB1 allows for three distinct proteins to be made, Kvß1.1, Kvß1.2, and Kvß1.3. Each of these has a unique N terminus. Kvβ1.1 is a cytoplasmic subunit that modulates the characteristics of the membrane spanning, channel-forming alpha-subunits. Beta subunits can promote the closure of channels or enhance channel activity depending on the channel members. Kvß1 is predominantly expressed in brain and found in hippocampus, cerebral cortex, caudate putamen, colliculus and cerebellum. Diseases associated with this gene include Episodic Ataxia, Type 1 and Familial Temporal Lobe Epilepsy, 3
Purified by Protein A chromatography
ICC, IHC, IP, WB
Synthetic peptide amino acids 7-28 (unique N-terminus) of rat Kv1.1 (TEHNLKSRNGEDRLLSKQSST; accession number NP_058999)
Human, Mouse, Non-Human Primate, Rat
Aliquot and store at ≤ -20°C for long term storage. For short term storage, store at 2-8°C. For maximum recovery of product, centrifuge the vial prior to removing the cap.
Produced by in vitro bioreactor culture of hybridoma line followed by Protein A affinity chromatography. Purified mAbs are >90% specific antibody.
10 mM Tris, 50 mM Sodium Chloride, 0.065% Sodium Azide pH 7.4
Does not cross-react with Kvβ1.2, Kvβ1.3, Kvβ2
Each new lot of antibody is quality control tested by IHC on either rat or mouse brain and confirmed to give the expected staining pattern.
These antibodies are to be used as research laboratory reagents and are not for use as diagnostic or therapeutic reagents in humans.
Ovsepian, S. V., et al. 2013. A defined heteromeric KV1 channel stabilizes the intrinsic pacemaking and regulates the output of deep cerebellar nuclear neurons to thalamic targets.. The Journal of Physiology, 1771-91.
Tipparaju, S. M., et al. 2012. Interactions between the C-terminus of Kv1.5 and Kvβ regulate pyridine nucleotide-dependent changes in channel gating.. Pflügers Archiv: European Journal of Physiology, 799-818.