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Validated All-in-One™ qPCR Primer for ANK1(NM_000037.4) Search again
Powered by BiozBy default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
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. [provided by RefSeq].
Gene References into function
- ankyrin and protein 4.1 are cleaved by native and recombinant falcipain-2 near their C-termini
- interaction of hydrophilic domain with two N-terminal immunoglobulin domains of titin
- A small muscle-specific isoform of the ANK1 gene, ank1.5, interacts with obscurin. Since ank1.5 is localised on the sarcoplasmic reticulum and obscurin on the myofibrils, these two proteins may provide a molecular link between these subcellular regions.
- identification of ankyrin as a target of spectrin's E2/E3 activity
- The interactions of three protein 4.2-derived recombinant proteins with CDB3 and ankyrin were investigated by using Far-Western blot and pull-down assay.
- off rates of the band 3-ankyrin interaction are sufficiently slow to allow sustained erythrocyte deformation without loss of elasticity
- Allelic and genotypic frequencies were similar in both studied groups for the G199A and Memphis I polymorphismsin Hereditary Spherocytosis among the Mexican population.
- It was shown that the region within beta-spectrin involved in interactions with ankyrin includes a lipid-binding site and binding is inhibited by ankyrin. Our results shows: the ankyrin-sens. lipid-bind. site of beta-spectrin exhibits a helical conform.
- Our results therefore indicate the importance of N-terminal region for lipid-binding activity of the beta-spectrin ankyrin-binding domain and its substantial role in maintaining the spectrin-based skeleton distribution.
- Structural and mutational studies of the binding region on small Ank1 for obscurin suggest that it consists of two ankyrin repeats with very similar structures.
- Ankyrin facilitates intracellular trafficking of alpha1-Na+-K+-ATPase in polarized cells.