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Immunogen sequence: SLLHQFQADA DDIDAWMLDI LKIVSSSDVG HDEYSTQSLV KKHKDVAEEI ANYRPTLDTL HEQASALPQE HAESPDVRGR LSGIEERYKE VAELTRLRKQ ALQDTLALYK MFSEADACEL WIDEKE
Highest antigen sequence identity to the following orthologs: Mouse - 94%, Rat - 94%.
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-G spectrin; Beta-II spectrin; beta-spectrin 2; beta-spectrin II; beta-spectrin non-erythrocytic 1; embryonic liver beta-fodrin; embryonic liver fodrin beta chain; epididymis luminal protein 102; Fodrin beta chain; spectrin beta chain, brain 1; Spectrin beta chain, non-erythrocytic 1; spectrin, beta, non-erythrocytic 1; Spectrin, non-erythroid beta chain 1
Gene Aliases: betaSpII; ELF; HEL102; SPTB2; SPTBN1
UniProt ID: (Human) Q01082
Entrez Gene ID: (Human) 6711
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