KCNE2 Protein, Human (Cell-Free, His)

The KCNE2 protein acts as an auxiliary subunit in voltage-gated potassium channels, affecting gating kinetics and channel stability. It regulates KCNB1, affects delayed rectifier voltage-dependent potassium channels, and cooperates with KCNH2/HERG to form the rapidly activating component of cardiac delayed rectifier potassium current (IKr). KCNE2 Protein, Human (Cell-Free, His) is the recombinant human-derived KCNE2 protein, expressed by E. coli Cell-free , with N-10*His labeled tag. The total length of KCNE2 Protein, Human (Cell-Free, His) is 123 a.a., with molecular weight of 17.3 kDa.

The KCNE2 protein serves as an ancillary subunit that forms a beta subunit within voltage-gated potassium channel complexes alongside pore-forming alpha subunits. By doing so, it plays a pivotal role in modulating the gating kinetics and enhancing the stability of the channel complex. When assembled with KCNB1, it influences the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1. In conjunction with KCNH2/HERG, KCNE2 is implicated in the formation of the rapidly activating component of the delayed rectifying potassium current in the heart (IKr). Furthermore, it may associate with KCNQ2 and/or KCNQ3, modulating the native M-type current, and interact with HCN1 and HCN2 to increase potassium current. KCNE2 is known to form heterooligomer complexes with various potassium channels, including KCNQ1 and KCNC2, leading to diverse functional outcomes. Additionally, it associates with Na(+)-coupled myo-inositol symporter in the apical membrane of choroid plexus epithelium, regulating the myo-inositol gradient between blood and cerebrospinal fluid with implications for neuron excitability. These intricate interactions underscore the versatile regulatory role of KCNE2 in modulating potassium currents and channel behavior.

Human

E. coli Cell-free

N-10*His

Q9Y6J6 (M1-P123)

9992

MSTLSNFTQTLEDVFRRIFITYMDNWRQNTTAEQEALQAKVDAENFYYVILYLMVMIGMFSFIIVAILVSTVKSKRREHSNDPYHQYIVEDWQEKYKSQILNLEESKATIHENIGAAGFKMSP

17.3 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.