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anti-Human Erythrocyte Ankyrin Antikörper:
anti-Rat (Rattus) Erythrocyte Ankyrin Antikörper:
anti-Mouse (Murine) Erythrocyte Ankyrin Antikörper:
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Human Polyclonal Erythrocyte Ankyrin Primary Antibody für IP, WB - ABIN4280780
Hall, Lu, Godfrey, Antonov, Paicu, Moxon, Dalmay, Wilczynska, Muller, Bushell: The cytoskeleton adaptor protein ankyrin-1 is upregulated by p53 following DNA damage and alters cell migration. in Cell death & disease 2016
Show all 2 Pubmed References
Cow (Bovine) Polyclonal Erythrocyte Ankyrin Primary Antibody für ELISA - ABIN314840
Dubreuil: Functional links between membrane transport and the spectrin cytoskeleton. in The Journal of membrane biology 2006
Our finding suggested that a de novo nonsense mutation in ANK1 may be causative to HS which plays an important role in supplementing the mutational spectrum of the ANK1 and explaining the mechanism of HS.
ANK1 rs508419-C type 2 diabetes (T2D)-risk allele alters DNA-protein complex binding leading to increased promoter activity and sAnk1 expression; thus, increased sAnk1 expression in skeletal muscle might contribute to T2D susceptibility.
rs515071 in ANK1 is a novel genetic risk for late-onset Alzheimer's disease susceptibility in Han Chinese.
The present study demonstrates that ANK1 is aberrantly expressed in pancreatic adenocarcinomas in association with promoter hypomethylation
Transient Receptor Potential Vanniloid-1 channel (TRPV-1 (zeige TRPV1 Antikörper)) has a role in the cough reflex and airway expression is increased in patients with chronic cough. The Ankyrin-1 receptor (TRPA-1 (zeige TRPA1 Antikörper)) is often co-expressed
Aberrant ANK1 methylation is highly prevalent in lung cancer, discriminate tumors by histology and patients' smoking history, and contributes to miR (zeige MLXIP Antikörper)-486-5p repression.
Study shows that Ankyrin-1 forms a high-affinity interaction with AE1 (zeige SLC4A1 Antikörper) tetramers but does not associate with AE1 (zeige SLC4A1 Antikörper) dimers in erythrocyte membranes.
ANK1 is up-regulated 4-fold in Alzheimer disease microglia, but not in neurons or astrocytes from the same individuals.
Two novel mutations in ANK1 (Y216X and E142X) are responsible for hereditary spherocytosis.
These results suggest that sAnk1 interacts with SLN (zeige SLN Antikörper) both directly and in complex with SERCA1 (zeige ATP2A1 Antikörper) and reduces SLN's inhibitory effect on SERCA1 (zeige ATP2A1 Antikörper) activity.
Parasites in ankyrin-1 (Ank-1) mutation erythrocytes grew normally, but red cells showed resistance to merozoite invasion.
This study highlights the first direct examination of allelic heterogeneity of the Ank-1 gene in the context of malaria resistance in mouse models.
With increasing age (at 12-15 mo of age) extensor digitorum longus (EDL (zeige LIPG Antikörper)) skeletal muscles of sAnk1 KO mice develop prematurely large tubular aggregates.
Study shows a direct interaction between beta-III spectrin (zeige SPTBN2 Antikörper) and erythroid ankyrin in the cerebellum and to demonstrate a critical role for beta-III spectrin (zeige SPTBN2 Antikörper) 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 (zeige HAMP Antikörper) 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 (zeige SLC4A1 Antikörper) 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.
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