Positive Control: SW1990 cell lysate, PANC-1 cell lysate, rat brain tissue lysate, mouse brain tissue lysate, mouse cerebellum tissue lysate, rat kidney tissue, human liver carcinoma tissue, mouse brain tissue.
Subcellular Location: Cell membrane, Cytoplasm, Cytoskeleton, Membrane.
Spectrin (Sp), the most abundant of the erythrocyte membrane skeleton proteins, helps these cells maintain their characteristic biconcave shape while remaining flexible and elastic. Erythrocyte Sp is a heterodimer composed of a 280 kDa alpha subunit and a 246 kDa beta subunit which associate in a side-to-side, antiparallel configuration to form a 100 nm rod-like structure. Sp in other tissues may be composed of distinct but homologous alpha and beta subunits, sometimes referred to as fodrin. A newly introduced nomenclature designates the Sp subunits of the erythrocyte as alpha-1 and beta-1, and the fodrin subunits as alpha-2 and beta-2. Alternatively spliced forms of each are designated as epsilon-1, epsilon-2, etc. (e. g. beta-1 epsilon-1).
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: beta fodrin; beta II spectrin-like (short form); beta-fodrin; beta-G spectrin; Beta-II spectrin; beta-spectrin 2; beta-spectrin 2, non-erythrocytic; beta-spectrin II; beta-spectrin non-erythrocytic 1; brain spectrin; bSPII-; cytoskeleton protein; embryonic liver beta-fodrin; Embryonic liver fodrin; embryonic liver fodrin beta chain; epididymis luminal protein 102; Fodrin beta chain; non-erythrocytic; non-erythroid spectrin beta; short form of beta II spectrin; spectrin beta 2; spectrin beta chain, brain 1; Spectrin beta chain, non-erythrocytic 1; spectrin G; spectrin, beta, non-erythrocytic 1; Spectrin, non-erythroid beta chain 1
Gene Aliases: 9930031C03Rik; AL033301; betaSpII; ELF; elf1; elf3; HEL102; mKIAA4049; Spnb-2; Spnb1; Spnb2; SPTB2; SPTBN1