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Potassium inwardly rectifying channel subfamily J member 11 (KCNJ11) is the core subunit of double transmembrane channel encoded by KCNJ11 gene. This subunit can form the core pore structure of ATP-sensitive potassium channel (KATP) on the cell membrane of islet β cells and neurons through tetramer assembly. The KCNJ11 polypeptide chain contains two transmembrane helices and intracellular conserved ATP binding pockets, and the extracellular loop structure forms an ion-selective filter, and its unique topological structure is different from the soluble cytoplasmic regulatory protein without membrane structure. Biochemical research confirmed that KCNJ11 needs to be combined with SUR regulatory subunit to form a complete KATP functional complex. When the energy level of cells increases, cytoplasmic ATP binds to KCNJ11 pocket site, which induces channel closure and realizes the precise regulation of ion channels by energy state.
The gene sequence variation of ATP binding domain in KCNJ11 cell can change the sensitivity of channel to nucleotide, resulting in abnormal shift of resting membrane potential of islet cells. Although Kir proteins in the same family have some inward rectification characteristics, there is no other Kir subunit that can completely replace the ATP sensing and pore regulation functions of KCNJ11 in KATP complex. As a typical integrated membrane protein, KCNJ11 is completely embedded in the lipid bilayer of cell membrane, and it must be tetrameric assembled with SUR subunit to play its biological function, which is essentially different from soluble cytoplasmic metabolism sensor.
KCNJ11 has dual functions of ATP-dependent gating regulation and potassium ion selective permeability. When the mutation of KCNJ11 leads to the decrease of ATP binding capacity, the channel will remain open continuously, which will inhibit the cell secretion function. Therefore, this channel subunit is an important core target for studying the mechanism of metabolic sensitive ion channels and analyzing the coupling relationship between energy metabolism and cell electrophysiology.
Fig. 1 Structural and cellular overview of the pancreatic KATP channel complex formed by KCNJ11 (Kir6.2) and SUR1 subunits, showing topology, conformational changes and cellular trafficking processes.1
The biological functions of integral membrane KCNJ11 Kir6.2 pore subunit are focused on nucleotide-dependent gating and potassium ion conduction:
Creative Biolabs offers purified KCNJ11 membrane protein samples produced under unified preparation workflows, including full-length KCNJ11 constructs and selected cytoplasmic domain variants. Truncated fragments cannot support complete channel assembly or ATP-dependent gating, while full-length forms are suitable for structural and biochemical studies of the Kir6.2 subunit. All batches receive uniform quality screening. Functional assessment of complete KATP channel gating and electrophysiological activity requires co-expression of KCNJ11 with SUR subunits, such as SUR1/ABCC8, in an appropriate membrane or cellular system. Pore, selectivity filter, and nucleotide-interaction features of KCNJ11 can be examined in comparative structural and biochemical studies. Full-length KCNJ11 samples support analysis of ATP interaction, subunit assembly, and Kir6.2-specific structural properties relevant to KATP channel research.
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Creative Biolabs provides cell research models with adjustable KCNJ11 expression levels, suitable for structural observation of Kir inward rectifier subunits and metabolic ion channel research. Sample assessment covers sustained membrane detection and tetramer assembly analysis, enabling side-by-side comparison of ATP gating behavior under varying KCNJ11 abundances. These cell models can be paired with membrane potential recording schemes to track secretory activity shifts linked to channel dosage changes.
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Anti-KCNJ11 recombinant antibodies are generated via standardized workflows, compatible with pancreatic cell membrane localization mapping and KATP tetramer complex identification. The antibody series supports multi-dimensional visualization of KCNJ11 distribution within endocrine tissue samples.
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Beyond catalog products, Creative Biolabs offers specialized custom services for KCNJ11 research:
KCNJ11 may act as an integral two-transmembrane pore subunit to assemble KATP channels and mediate ATP-sensitive selective potassium permeation.
KCNJ11 expression status might alter endocrine cell membrane potential and secretory output, serving as a key mediator of metabolic ion signaling biological processes.
No, all KCNJ11 related products and services are strictly for research use only, and cannot be applied in clinical workflows. All material design and functional screening are optimized exclusively for basic laboratory research, without meeting clinical application criteria.
Offerings include full-length KCNJ11 membrane protein, target-specific recombinant antibodies and tunable expression cell research models, supporting research on Kir tetramer assembly and ATP-gated ion flux transduction.
Laboratory analysis schemes may include potassium conductance recording assays to assess nucleotide-dependent pore activity under simulated lipid bilayer environments.