Anti-Kcnn4 Antibody Picoband®

Intermediate conductance calcium-activated potassium channel protein 1 (KCNN4, Kca3.1) is part of a potentially heterotetrameric voltage-independent potassium channel that is activated by intracellular calcium. Activation is followed by membrane hyperpolarization, which promotes calcium influx. KCNN4 may be part of the predominant calcium-activated potassium channel in T-lymphocytes. This gene is similar to other KCNN family potassium channel genes, but it differs enough to possibly be considered as part of a new subfamily.

Intermediate conductance calcium-activated potassium channel protein 4; SK4; SKCa 4; SKCa4; IKCa1; IK1; KCa3.1; KCa4; Putative Gardos channel; KCNN4; IK1; IKCA1; KCA4; SK4

Forms a voltage-independent potassium channel that is activated by intracellular calcium (PubMed:26148990) . Activation is followed by membrane hyperpolarization which promotes calcium influx. Required for maximal calcium influx and proliferation during the reactivation of naive T-cells. The channel is blocked by clotrimazole and charybdotoxin but is insensitive to apamin (PubMed:17157250, PubMed:18796614) .

1. Joiner WJ, Wang LY, Tang MD, Kaczmarek LK. Joiner, W.J., Wang, L.Y., Tang, M.D. and Kaczmarek, L.K. hSK4, a member of a novel subfamily of calcium-activated potassium channels. Proc. Natl. Acad. Sci. U.S.A.1997; 94 (20), 11013-11018. 2. Hoffman JF, Joiner W, Nehrke K, Potapova O, Foye K, Wickrema A. The hSK4 (KCNN4) isoform is the Ca2+-activated K+ channel (Gardos channel) in human red blood cells. Proc. Natl. Acad. Sci. U.S.A.2003; 100 (12), 7366-7371. 3. Jones HM, Hamilton KL, Papworth GD, Syme CA, Watkins SC, Bradbury NA, Devor DC. Role of the NH2 terminus in the assembly and trafficking of the intermediate conductance Ca2+-activated K+ channel hIK1. J. Biol. Chem.2004; 279 (15), 15531-15540.

At -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freezing and thawing.