SPTAN1 antibody

Catalog No. ABIN1580410

Product Details anti-SPTAN1 Antibody

Target: SPTAN1 (Spectrin alpha Chain, Brain (SPTAN1))

Reactivity: Human

Host: Mouse

Clonality: Monoclonal

Conjugate: This SPTAN1 antibody is un-conjugated

Application: Western Blotting (WB), Immunohistochemistry (IHC), Immunocytochemistry (ICC), Immunofluorescence (IF)

Purification: affinity purified antibody

Clone: 3D7

Isotype: IgG1

Application Details

Application Notes: The antibody preparation can be diluted to 1:500-1,000 for immunofluorescence staining and 1:5,000-10,000 for western blotting. On western blots look for a major band at 240 kDa, depending on the species.

Restrictions: For Research Use only

Handling

Format: Liquid

Concentration: 1 mg/mL

Handling Advice: Avoid repeated freezing and thawing.

Storage: 4 °C/-20 °C

Storage Comment: Store at 4°C short term or -20°C long term.

Target Details for SPTAN1

Target: SPTAN1 (Spectrin alpha Chain, Brain (SPTAN1))

Alternative Name: alpha-II spectrin (SPTAN1 Products)

Synonyms: im:7157190 antibody, wu:fa20e05 antibody, wu:fb33g08 antibody, wu:fk32a10 antibody, zgc:112229 antibody, 2610027H02Rik antibody, Spna-2 antibody, Spna2 antibody, EIEE5 antibody, NEAS antibody, SPTA2 antibody, A2a antibody, IPF antibody, SPECA antibody, spectrin alpha, non-erythrocytic 1 antibody, spectrin, alpha, non-erythrocytic 1 antibody, SPTAN1 antibody, sptan1 antibody, Sptan1 antibody

Background: The spectrin family of proteins were originally discovered as major components of the submembraneous cytoskeleton of osmotically lysed red blood cells. The lysed blood cells could be seen as clear red blood cell shaped objects in the light microscope and were referred to as red cell ghosts. The major proteins of these ghosts proved to be actin, ankyrin, band 4.1 and several other proteins, including two major bands running at about 240 kDa and 260 kDa on SDS-PAGE gels. This pair of bands was named spectrin since they were discovered in these red blood cell ghosts. Later work showed that similar high molecular bands were seen in membrane preparations from other eukaryotic cell types. Work by Levine and Willard described a pair of about approx. 240-260 kDa molecular weight bands which were transported at the slowest rate along mammalian axons. They named these proteins fodrin as antibody studies showed that they were localized in the sheath under the axonal membrane, but not in the core of the axon. Subsequently, fodrin was found to be a member of the spectrin family of proteins, and the spectrin nomenclature is now normally used. Spectrins form tetramers of two alpha, and two beta, subunits, with the alpha, corresponding to the lower molecular weight approx. 240 kDa band and the beta, corresponding to the approx. 260 kDa or in some case much larger band. Most spectrin tetramers are about 0.2 microns or 200 nm long, and each alpha, and beta, subunit has a cell type specific expression pattern. The basic structure of each spectrin subunit is the spectrin repeat, which is a sequence of about 110 amino acids which defines a compact domain contain three closely packed alpha,-helices. Each spectrin subunit contains multiple copies of this repeat, with 20 in each of the alpha, subunits. The beta, I-IV subunits each contain 17 spectrin repeats, while the beta, V subunit, also known as beta,-heavy spectrin, contains 30 of these repeats. The various subunits also contain several other kinds of functional domains, allowing the spectrin tetramer to interact with a variety of protein, ionic and lipid targets. The alpha,-subunits each contain one calmodulin like calcium binding region and one Src-homology 3 (SH3) domain, an abundant domain involved in specific protein-protein interactions. The beta, subunits all have a N-terminal actin binding domain and may also have one SH3 domain and one pleckstrin homology domain, a multifunctional type of binding domain which in beta, I spectrin at least binds the membrane lipid PIP2. Spectrins are believed to have a function in giving mechanical strength to the plasma membrane since the tetramers associate with each other to form a dense submembraneous geodesic meshwork. They also bind a variety of other membrane proteins and membrane lipids, and the proteins they bind to are therefore themselves localized in the membrane. Diseases may be associated with defects in one or other of the spectrin subunits. For example, some forms of hereditary spherocytosis, the presence of spherical red blood cells which are prone to lysis, can be traced to mutations in some of the spectrin subunits. The alpha,-II subunit is widely expressed in tissues but, in the nervous system, is found predominantly in neurons. Our antibody can therefore be used to identify neurons and fragments derived from neuronal membranes in cells in tissue culture and in sectioned material. This antibody was raised against a recombinant construct containing the seventh, eighth and ninth of the so-called spectrin repeats. The HGNC name for this protein is SPTAN1.

Pathways: Caspase Cascade in Apoptosis, Regulation of Actin Filament Polymerization