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Mammalian Monoclonal ANK2 Primary Antibody für ISt, IHC - ABIN1304531
Huff, Shi, Sun, Wu, Shi, Cheng: Real-time CARS imaging reveals a calpain-dependent pathway for paranodal myelin retraction during high-frequency stimulation. in PLoS ONE 2011
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Mammalian Monoclonal ANK2 Primary Antibody für ISt, IHC - ABIN1304530
Chang, Zollinger, Susuki, Sherman, Makara, Brophy, Cooper, Bennett, Mohler, Rasband: Glial ankyrins facilitate paranodal axoglial junction assembly. in Nature neuroscience 2014
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Human Monoclonal ANK2 Primary Antibody für FM, ELISA - ABIN967633
Scotland, Zhou, Benveniste, Bennett: Nervous system defects of AnkyrinB (-/-) mice suggest functional overlap between the cell adhesion molecule L1 and 440-kD AnkyrinB in premyelinated axons. in The Journal of cell biology 1999
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Cell-autonomous adiposity results from increased cell surface GLUT4 due to ankyrin-B deficiency in humans and mice.
The authors discovered that the entire 24 ankyrin repeats are inhibited by combinatorial and quasi-independent bindings of multiple disordered segments located in the ankyrin-B/G linkers and tails, suggesting a mechanistic basis for differential regulations of membrane target bindings by ankyrins.
we support classification of Ankyrin-B p.L1622I as a "mild" loss-of-function variant that may confer arrhythmia susceptibility in the context of secondary risk factors including environment, medication, and/or additional genetic variation.
Clinical manifestations of ANK2 variants may include QT prolongation and torsades de pointes, often precipitated by strenuous exercise or stress.
Disruption of Ankyrin B and Caveolin-1 Interaction Sites Alters Na(+),K(+)-ATPase Membrane Diffusion
Report disease-causing ANK2 variant localized to the membrane-binding domain resulting in reduced ankyrin-B expression and abnormal localization in a First Nations population with a high rate of long QT syndrome.
VariousANK2mutations are associated with a wide range of phenotypes, including aLQTS, especially with ventricular fibrillation, representing "ankyrin-B" syndrome.
Rare Variants in ANK2 Associated With Various Inherited Arrhythmia Syndromes.
The identification and characterization of two functionally distinct ankyrin-B isoforms in heart provide compelling evidence that alternative splicing of the ANK2 gene regulates the fidelity of ankyrin-B interactions with proteins
the structures of ANK repeats in complex with an inhibitory segment from the C-terminal regulatory domain and with a sodium channel Nav1.2 peptide, are reported.
Gankyrin plays an essential role in estrogen-driven and GPR30-mediated endometrial carcinoma cell proliferation via the PTEN/PI3K/AKT signaling pathway.
ankyrin-B linker suppresses activity of the ANK repeat domain through an intramolecular interaction, likely with a groove on the surface of the ANK repeat solenoid, thereby regulating the affinities between ankyrin-B and its binding partners
Residues 63-73 of cdB3 is also essential for ankyrin binding.
Ankyrin-B protein in heart failure: identification of a new component of metazoan cardioprotection.
Reduced ankyrin-B expression or mutations in ankyrin 2 are associated with atrial fibrillation.
Data show that DAnk2-binding is critical for beta spectrin function in vivo.
This protein has been found differentially expressed in thalami from patients with schizophrenia.
The common genetic variation in the ANK2 gene is modified the physiological variability of the QT interval in the general population.
The ankyrin-B C-terminal domain determines activity of ankyrin-B/G chimeras
Loss-of-function (E1425G) mutation in ankyrin-B (also known as ankyrin 2), a member of a family of versatile membrane adapters, causes dominantly inherited type 4 long-QT cardiac arrhythmia in humans
These findings reveal spectrin (alpha/beta) / ankyrin B cytoskeletal and signaling proteins as key regulators of T-type calcium channels expressed in the nervous system.
We demonstrate that AnkB binds to Rab GTPase Activating Protein 1-Like (RabGAP1L) and recruits it to PI3P-positive organelles, where RabGAP1L inactivates Rab22A, and promotes polarized trafficking to the leading edge of migrating fibroblasts. We further determine that a5b1-integrin depends on an AnkB/RabGAP1L complex for polarized recycling
The increased incidence of pro-arrhythmogenic Ca(2+) sparks and waves in AnkB(+/-) hearts is due to enhanced CaMKII-mediated RyR phosphorylation, which is caused by higher junctional [Ca(2+)] and consequent local CaMKII activation.
Taken together, these observations reveal that AnkB is required for Prx membrane anchoring and for maintenance of lens fiber cell hexagonal geometry, membrane skeleton organization, and biomechanics.
that ankyrin-B deficiency results in a metabolic syndrome that combines primary pancreatic beta cell insufficiency with peripheral insulin resistance
Functional relationships between PIK3C3, dynactin, and AnkB promote axonal transport of organelles and are required for normal axon length.
These findings identify an interaction between ankyrin-B and both Cav2.1 and Cav2.2 at the amino acid level that is necessary for proper Cav2.1 and Cav2.2 targeting in vivo.
AnkB reduction alters cardiac Na and Ca transport and enhances the coupled RyR openings, resulting in more frequent Ca sparks and waves although the total SR Ca leak is unaffected.
Ankyrin-B then interacts with dynactin-4 and dystrophin, whereas dynactin-4 collaborates with dystrophin in coordinating costamere-aligned microtubules
Ankyrin-B regulates Kir6.2 membrane expression and function in heart.
Findings highlight the importance of the functional anatomy of the entire atrial distributed pacemaker complex and clearly demonstrate the role of AnkB in cardiac automaticity.
Defective glycemic regulation through loss of ankyrin-B-dependent stabilization of IP3R is a potential risk factor for type 2 diabetes.
Mice heterozygous for a null mutation in ankyrin-B are haploinsufficient and display arrhythmia similar to humans
ankyrin-B has a role in Inositol 1,4,5-trisphosphate receptor localization and stability in neonatal cardiomyocytes
We propose that the ankyrin-B-based complex is a specialized adaptation of cardiomyocytes with a role for cytosolic Ca2+ modulation
Ankyrin-B has a role in cardiac function, cardiac death and premature senescence
This gene encodes a member of the ankyrin family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton. Ankyrins play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Most ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple ankyrin repeats\; a central region with a highly conserved spectrin binding domain\; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. The protein encoded by this gene is required for targeting and stability of Na/Ca exchanger 1 in cardiomyocytes. Mutations in this gene cause long QT syndrome 4 and cardiac arrhythmia syndrome. Multiple transcript variants encoding different isoforms have been described.
, ankyrin, brain
, ankyrin-2, nonerythrocytic
, non-erythroid ankyrin
, brain ankyrin
, ankyrin 2, brain
, ankyrin 3, epithelial
, ankyrin 2, neuronal