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Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Additionally we are shipping Erythrocyte Ankyrin Antibodies (53) and and many more products for this protein.
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Ankyrin-1 is induced to a greater extent than the embedded miRNA following DNA damage.
analysis of a novel p.Q1772X ANK1 mutation in a Korean family with hereditary spherocytosis [case report of two family members]
The study reports the refinement for a protein heterodimer complex using limited EPR (show EREG ELISA Kits) spectroscopic data and a rigid-body docking algorithm: a three-dimensional model for an ankyrin 1-BND3 (show SLC4A1 ELISA Kits) complex.
A novel L1340P mutation in the ANK1 gene is associated with hereditary spherocytosis.
Our analyses suggest that these DNA methylation (show HELLS ELISA Kits) changes may have a role in the onset of Alzheimer disease given that we observed them in presymptomatic subjects and that six of the validated genes connect to a known susceptibility gene network.
We identified a differentially methylated region in the ankyrin 1 (ANK1) gene that was associated with neuropathology in the entorhinal cortex, a primary site of Alzheimer disease manifestation.
ANK1 rs516946 confers impaired insulin (show INS ELISA Kits) release.
The ankyrin-binding site on band 3 (show SLC4A1 ELISA Kits) is located near the deoxygenated hemoglobin (show HBB ELISA Kits)-binding site, therefore following deoxygenation ankyrin is displaced from band 3 (show SLC4A1 ELISA Kits).
A tissue-specific chromatin loop brings NF-E2 (show NFE2 ELISA Kits) and ANK1E into close proximity preventing gene silencing and mutagenesis leading to hereditary spherocytosis.
results indicate that the ANK1 locus is a new, common susceptibility locus for type 2 diabetes across different ethnic groups
With increasing age (at 12-15 mo of age) extensor digitorum longus (EDL (show LIPG ELISA Kits)) skeletal muscles of sAnk1 KO mice develop prematurely large tubular aggregates.
Study shows a direct interaction between beta-III spectrin (show SPTBN2 ELISA Kits) and erythroid ankyrin in the cerebellum and to demonstrate a critical role for beta-III spectrin (show SPTBN2 ELISA Kits) in maintaining ankyrin R throughout the Purkinje cell dendritic tree.
Hema6 mutation of ankyrin-1 causes hereditary spherocytosis in mice through a mild reduction of protein expression.
Suppression of hepcidin (show HAMP ELISA Kits) expression and iron overload mediate Salmonella susceptibility in ankyrin 1-mutated mice.
We conclude that increased malaria resistance due to ankyrin-1 deficiency is caused by the intraerythrocytic death of P. chabaudi parasites.
These results demonstrate that mammalian erythroblast enucleation does not depend on the membrane integrity generated by the ankyrin-band 3 (show SLC4A1 ELISA Kits) complex.
The Ank1(E924X) strain provides a novel tool to study Ank1 and model HS.
A spontaneous mutation, normoblastosis (Ank1nb) in mice provides an important animal model for human ankyrin-deficient anemias.
Results support a role of obscurin (show OBSCN ELISA Kits) in mediating the subcellular localization of small ankyrin1 isoforms in striated (show NSDHL ELISA Kits) muscle cells.
the organization of obscurin (show OBSCN ELISA Kits) at different locations in the sarcomere changes during muscle development and that this might affect the interaction with ank1.5.
Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Multiple isoforms of ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. 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. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of ankyrin 1 have been described. Truncated muscle-specific isoforms of ankyrin 1 resulting from usage of an alternate promoter have also been identified.
ankyrin 1, erythrocytic
, erythroid ankyrin
, erythrocyte ankyrin
, ankyrin 1, erythroid
, normoblastic anemia