epitope corresponding to amino acids 541-650 of spectrin α I of human origin
Modification Notes
Spectrin, an Actin binding protein that is a major component of the cytoskeletal superstructure of the erythrocyte plasma membrane, is essential in determining the properties of the membrane including its shape and deformability. Spectrins function as membrane organizers and stabilizers, composed of non-homologous a and b chains, which aggregate side-to-side in an antiparallel fashion to form dimers, tetramers and higher polymers. Spectrin a I and spectrin b I are present in erythrocytes, whereas spectrin a II (also designated fodrin a) and spectrin b II (also designated fodrin b) are present in other somatic cells. The spectrin tetramers in erythrocytes act as barriers to lateral diffusion, but spectrin dimers seem to lack this function. Defects of spectrin a I are present in the erythrocytes of many patients with abnormalities of red blood cell shape including hereditary spherocytosis and elliptocytosis.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of spectrin α I of mouse, rat and human origin by WB, IP, IF and ELISA:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 541-650 of spectrin &alpha I of human origin
Tissue Specificity
epitope corresponding to amino acids 541-650 of spectrin α I of human origin