Anti-Ankyrin erythroid/ANK/ANK1 Antibody Picoband® (monoclonal, 9I6C3)

Ankyrin 1, erythrocytic, also known as ANK1, is a protein that in humans is encoded by the ANK1 gene. 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.

Histone-binding protein RBBP4; Chromatin assembly factor 1 subunit C; CAF-1 subunit C; Chromatin assembly factor I p48 subunit; CAF-I 48 kDa subunit; CAF-I p48; Nucleosome-remodeling factor subunit RBAP48; Retinoblastoma-binding protein 4; RBBP-4; Retinoblastoma-binding protein p48; RBBP4; RBAP48

Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex.

1. Davies, K. A., Lux, S. E. Hereditary disorders of the red cell membrane skeleton. Trends Genet. 5: 222-227, 1989. 2. Duru, F., Gurgey, A., Ozturk, G., Yorukan, S., Altay, C. Homozygosity for dominant form of hereditary spherocytosis. Brit. J. Haemat. 82: 596-600, 1992. 3. Eber, S. W., Gonzalez, J. M., Lux, M. L., Scarpa, A. L., Tse, W. T., Dornwell, M., Herbers, J., Kugler, W., Ozcan, R., Pekrun, A., Gallagher, P. G., Schroter, W., Forget, B. G., Lux, S. E. Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis. Nature Genet. 13: 214-218, 1996.

At -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freezing and thawing.