KCNJ11 antibody Host Goat
- Known as:
- KCNJ11 (anti-) Host Goat
- Catalog number:
- 'AP16735PU-N
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- ACR
- Gene target:
- KCNJ11 antibody Host Goat
Related genes to: KCNJ11 antibody Host Goat
- Gene:
- KCNJ11 NIH gene
- Name:
- potassium voltage-gated channel subfamily J member 11
- Previous symbol:
- -
- Synonyms:
- Kir6.2, BIR
- Chromosome:
- 11p15.1
- Locus Type:
- gene with protein product
- Date approved:
- 1997-09-12
- Date modifiied:
- 2018-03-06
Related products to: KCNJ11 antibody Host Goat
Related articles to: KCNJ11 antibody Host Goat
- Congenital hyperinsulinism (CHI) is characterized by inappropriate insulin secretion resulting in persistent neonatal hypoglycemia. CHI is often linked to mutations in the and genes and can lead to persistent hypoglycemia, seizures, and neurological injury, making early diagnosis and management essential. - Source: PubMed
Publication date: 2026/09/23
Kansakar PreranaGurung GrishaBhandari SadikshyaShrestha KritiG C BhumikaThapa ShreyaAcharya Rasik - Neuroendocrine ATP-sensitive K+ channels (KATP) comprise four pore-forming subunits (Kir6.2), each associated with a modulatory sulfonylurea receptor subunit (SUR1). ATP/ADP binding to Kir6.2 inhibits KATP; MgATP/MgADP binding to two different sites on SUR1 promotes activation. As SUR1 is a member of the ABC transporter family of proteins, it can potentially hydrolyze MgATP to MgADP. Whether this activity is required for KATP activation remains controversial. Previous studies demonstrated that non-hydrolyzable ATP analogs do not activate KATP, which may reflect an inability of these compounds to bind to SUR1, their inability to promote a conformational change in SUR1 that leads to channel activation, or a requirement for ATP hydrolysis during channel gating. To explore this further, we synthesized a fluorescent trinitrophenyl (TNP) derivative of the non-hydrolyzable ATP analog β,γ-methyleneadenosine 5'-triphosphate (AMP-PCP). Synthesis was verified by UV-visible absorbance, fluorescence spectroscopy, 1H NMR, and mass spectrometry. Purity was assessed by reversed-phase HPLC. Real-time nucleotide binding to intact KATP channels in cell membranes was measured using FRET between channels labeled with a fluorescent, noncanonical amino acid and TNP-nucleotide derivatives. This technique provides sufficient spatial resolution to discriminate between binding to each site on KATP. Using this approach, we first established that TNP-ATP can bind to nucleotide-binding site (NBS) 1 on SUR1 in fluorescently labeled Kir6.2/SUR1 channels in unroofed membranes of HEK293T cells. We subsequently demonstrated that TNP-AMP-PCP binds to both NBSs on SUR1 in the absence of Mg2+. AMP-PCP was able to compete with TNP-ATP for binding to NBS2, suggesting that it, too, binds NBS2. We conclude that the failure of non-hydrolyzable ATP analogs to activate KATP does not stem from an inability of these nucleotides to bind to the channel. - Source: PubMed
Publication date: 2026/09/18
Rubio PriscillaWhitaker Shayla QAshby JonathanPuljung Michael C - Mutations in ABCC8 and KCNJ11 are associated with the most severe and diazoxide-resistant forms of congenital hyperinsulinism (CHI). Somatostatin analogues are commonly used off-label as second-line treatment. While octreotide and lanreotide are the most established options, pasireotide-a second-generation somatostatin analogue with higher affinity for somatostatin receptor subtype 5-has been hypothesized to offer improved suppression of insulin secretion. We report the off-label use of subcutaneous pasireotide in an infant with severe CHI due to a homozygous ABCC8 mutation. The patient presented with severe persistent hypoglycemia despite high-dose octreotide, continuous glucagon infusion, and high carbohydrate requirement. The established next step would have been a subtotal pancreatectomy. Following detailed counseling, the parents expressed a strong preference to defer surgical intervention and to pursue further medical options. Thus, an individualized therapeutic trial with subcutaneous pasireotide was initiated at approximately 8 weeks of age as an attempt to avoid surgery. However, pasireotide at doses of up to 0.11 mg/kg/day administered every 4 h did not lead to substantial clinical improvement. Instead, treatment was associated with increased glycemic variability, as reflected by more frequent episodes of hypo- and hyperglycemia, ultimately requiring reintroduction of glucagon as rescue therapy. No adverse effects were observed. Due to the lack of therapeutic response, pasireotide was discontinued after 8 days and the patient underwent near-total pancreatectomy. In conclusion, intermittent pasireotide injections were not associated with clinical improvement in this infant with medically refractory CHI, and its use potentially contributed to increased glycemic variability and instability. Further studies are needed to evaluate the safety and efficacy of pasireotide in this vulnerable patient population. - Source: PubMed
Publication date: 2026/08/27
Kurz CalvinRoeper MarciaFriesl LisaMayatepek ErtanMeissner ThomasKummer SebastianHoermann HenrikeWelters Alena - Most antipsychotic drugs (APDs) cause hyperphagia and weight gain, yet the neural mechanisms underlying these metabolic side effects remain elusive, in part due to difficulties in modeling them in rodents. Here, we establish a mouse model that recapitulates clozapine-induced metabolic syndrome, enabling mechanistic investigation of this widely prescribed APD. We show that clozapine promotes obesity in female mice by driving hyperphagia, which requires functional coupling between the melanocortin 4 receptor (MC4R) and the Kir7.1 potassium channel. Within the broader context of clozapine's polypharmacology, this signaling axis emerges as a critical downstream convergence node for APD-induced metabolic dysfunction. Mechanistically, clozapine inhibits MC4R-expressing neurons in the paraventricular nucleus of the hypothalamus by enhancing MC4R-Kir7.1 coupling, thereby increasing inward potassium currents. Notably, clozapine produces this inhibition without binding the MC4R orthosteric site and without engaging canonical Gαs signaling. Genetic deletion of Kir7.1 in MC4R neurons or pharmacological inhibition of Kir7.1 reverses clozapine-induced weight gain while preserving its behavioral efficacy in established antipsychotic assays. Together, these findings reveal a G-protein-independent mechanism by which clozapine disrupts energy balance and identify MC4R-Kir7.1 coupling as a therapeutically tractable pathway for mitigating APD-associated metabolic dysfunction. - Source: PubMed
Publication date: 2026/09/03
Li LiHernandez Ciria CGimenez Luis EXu BaijieDahir Naima SPeisley AlysWu ZanChen MeilinSerrato AlexandraWan RongSwati Birnbaum Shari GCone Roger DLiu Chen - KirBac1.1 is a prokaryotic homolog of mammalian inward-rectifier potassium (Kir) channels, and the functional equilibrium of KirBac1.1 is highly dependent on the type of membrane lipids. Like Kir channels, KirBac1.1 activity is also inhibited by cholesterol, a physiologically relevant lipid in human health and disease. Despite the slide helix is an important functional motif during lipid-dependent gating, the structural dynamics of the slide helix during cholesterol-induced channel inactivation is not well understood and is the focus of this work. Sequence analysis reveals that the slide helix of KirBac1.1 itself is a putative cholesterol-recognition motif. Liposomal K+ flux assays show that transport activity of the wild-type channel in PC/PG membranes is completely abolished at high concentration of cholesterol, whereas this is not observed in some of the single-cysteine mutants of the slide helix, indicating slide helix residues are critical for cholesterol sensitivity. Quenching of intrinsic Trp fluorescence upon increasing cholesterol concentration strongly suggests that the KirBac1.1 functional inhibition by cholesterol is possibly due to its direct interaction with the channel. Membrane penetration depth measurements using NBD-labeled slide helix residues clearly show relatively shallow membrane interfacial localization of the slide helix in cholesterol-containing membranes that is associated with significant structural dynamics changes and altered conformational heterogeneity. Based on distance measurements in varying membrane lipid compositions that stabilize the active and inactive conformations, we hypothesize that slide helix position in the membrane might possibly act as a "conformational switch" in regulating the KirBac1.1 function. These results involving dynamic lipid-protein interactions in lipid-dependent gating might be relevant for other Kir channels. - Source: PubMed
Publication date: 2026/08/06
Bysack ArpanRaghuraman H