This Antibody was verified by Relative expression to ensure that the antibody binds to the antigen stated. View Details
Immunogen sequence: TSVLILQRKH KAFEDELRGL DAHLEQIFQE AHGMVARKQF GHPQIEARIK EVSAQWDQLK DLAAFCKKNL QDAENFFQFQ GDADDLKAWL QDAHRLLSGE DVGQDEGATR ALGKKHKDFL EELEESRGVM EHLEQQAQGF PEEF
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