Thermo Fisher Scientific Ankyrin erythroid Polyclonal Antibody

Applications

Tested Dilution

Publications

Immunohistochemistry (Paraffin) (IHC (P))

Assay-dependent

-

Immunohistochemistry (Frozen) (IHC (F))

1:100-1:500

-

Immunocytochemistry (ICC/IF)

1:50-1:200

-

ELISA (ELISA)

1:500-1:1,000

-

Product Specifications

Species Reactivity

Human, Mouse, Rat

Host/Isotype

Rabbit / IgG

Class

Polyclonal

Type

Antibody

Immunogen

KLH conjugated synthetic peptide derived from human Ankyrin erythroid, amino acids 501-600. if (typeof window.$mangular === undefined || !window.$mangular) { window.$mangular = {}; } $mangular.antigenJson = \[{targetFamily:Ankyrin 1,uniProtId:P16157-1,ncbiNodeId:9606,antigenRange:501-600,antigenLength:1881,antigenImageFileName:BS-7594R_Ankyrin_1_P16157-1_Rabbit.svg,antigenImageFileNamePDP:BS-7594R_Ankyrin_1_P16157-1_Rabbit_PDP.jpeg,sortOrder:1}\]; $mangular.isB2BCMGT = false; $mangular.isEpitopesModalImageMultiSizeEnabled = true;

View immunogen .st0{fill:#FFFFFF;} .st1{fill:#1E8AE7;}

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

1 mg/mL

Purification

Protein A

Storage buffer

0.01M TBS, pH 7.4, with 50% glycerol, 1% BSA

Contains

0.02% ProClin 300

Storage conditions

-20°C

Shipping conditions

Ambient (domestic); Wet ice (international)

Target Information

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.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.