Ankyrin B Mouse, Unlabeled, Clone: 2.2, BD

Description

• Ankyrins are a family of proteins which were first discovered in erythrocytes and shown to bind to spectrin, a primary component of the cytoskeletal architecture
• They have since been shown to be expressed at very high levels in the vertebrate brain and are also found in other cell types
• Ankyrins function by acting as adaptors to link integral membrane proteins, including cell adhesion and ion channel molecules to the cytoskeleton
• The structure of ankyrin consists of three domains, two highly conserved N-terminal and one C-terminal variable domain
• The conserved regions contain a membrane-binding domain of ∽89-95 kDa and a spectrin-binding domain of ∽62 kDa, while the variable region has pre-mRNA alternative splice sites
• Two ankyrins have been extensively characterized: ankryin R is the product of the ANK1 gene and is primarily expressed in the brain, although alternatively spliced forms are found in erythrocytes; ankyrin B is the product of the ANK2 gene, located on a different chromosome from ANK1, and is primarly expressed in neonatal and adult brain but is also found in heart, lymphocytes and platelets
• Studies done on ankyrinB (-/-) knockout mice, which die by postnatal day 21, have demonstrated a link between the L1 cell adhesion molecule and ankyrin B in premyelinated axons
• Isoforms of ankyrin B have been reported to be detectable ranging from approximately 440, 220, 150 and 110 kDa in western blot analysis, depending on the tissue-type of origin
• This antibody is routinely tested by western blot analysis
• Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.