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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 (show CA2 ELISA Kits)+) sparks and waves in AnkB (show ANKH ELISA Kits)(+/-) hearts is due to enhanced CaMKII (show CAMK2G ELISA Kits)-mediated RyR (show RYR1 ELISA Kits) phosphorylation, which is caused by higher junctional [Ca(2 (show CA2 ELISA Kits)+)] and consequent local CaMKII (show CAMK2G ELISA Kits) activation.
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
Taken together, these observations reveal that AnkB (show ANKH ELISA Kits) is required for Prx (show PRX ELISA Kits) 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 (show INS ELISA Kits) resistance
Functional relationships between PIK3C3 (show PIK3C3 ELISA Kits), dynactin (show DCTN1 ELISA Kits), and AnkB (show ANKH ELISA Kits) promote axonal transport of organelles and are required for normal axon length.
These findings identify an interaction between ankyrin-B and both Cav2.1 (show CACNA1A ELISA Kits) and Cav2.2 (show CACNA1B ELISA Kits) at the amino acid level that is necessary for proper Cav2.1 (show CACNA1A ELISA Kits) and Cav2.2 (show CACNA1B ELISA Kits) targeting in vivo.
Ankyrin-B protein (show LEPREL2 ELISA Kits) in heart failure: identification of a new component of metazoan cardioprotection.
AnkB (show ANKH ELISA Kits) reduction alters cardiac Na and Ca transport and enhances the coupled RyR (show RYR1 ELISA Kits) openings, resulting in more frequent Ca sparks and waves although the total SR Ca leak is unaffected.
Ankyrin-B then interacts with dynactin-4 (show DCTN5 ELISA Kits) and dystrophin (show DMD ELISA Kits), whereas dynactin-4 (show DCTN5 ELISA Kits) collaborates with dystrophin (show DMD ELISA Kits) in coordinating costamere-aligned microtubules
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 structures of ANK (show ANK1 ELISA Kits) repeats in complex with an inhibitory segment from the C-terminal regulatory domain and with a sodium channel Nav1.2 (show SCN2A ELISA Kits) peptide, are reported.
Gankyrin (show PSMD10 ELISA Kits) plays an essential role in estrogen-driven and GPR30 (show GPER ELISA Kits)-mediated endometrial carcinoma cell proliferation via the PTEN/PI3K (show PIK3CA ELISA Kits)/AKT (show AKT1 ELISA Kits) signaling pathway.
ankyrin-B linker suppresses activity of the ANK (show ANK1 ELISA Kits) repeat domain through an intramolecular interaction, likely with a groove on the surface of the ANK (show ANK1 ELISA Kits) repeat solenoid, thereby regulating the affinities between ankyrin-B and its binding partners
Residues 63-73 of cdB3 is also essential for ankyrin binding.
Reduced ankyrin-B expression or mutations in ankyrin 2 are associated with atrial fibrillation.
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 2, neuronal
, ankyrin repeat and zinc finger domain containing protein 1
, brain ankyrin
, ankyrin B
, ankyrin, brain
, ankyrin-2, nonerythrocytic
, non-erythroid ankyrin
, ankyrin 2, brain
, ankyrin 3, epithelial