Spectrin is a multifunctional protein that has lipid-binding sites within CH (calponin-homology) tandem domains, a PH (pleckstrin homology) domain and triple helical segments. It is located on chromosome 1q23.1.
Spectrin is the major cytoskeletal component in erythrocytes. It is composed of two types of polypeptides known as α and β with molecular weights of 240 and 220 kDa, respectively. The α- and β-chains form heterotetramers which are linked end-to-end via oligomeric actin and band 4.1 protein.
Specificity
The antibody reacts specifically with the α and β chains of human erythrocyte spectrin.
Immunogen
spectrin from freshly prepared human erythrocyte ghosts.
Application
Anti-Spectrin antibody has been used in western blotting immunofluorescence and immunostaining.
Biochem/physiol Actions
Spectrins modulates the cell morphology and mechanical properties. Spectrins also participates in the cell cycle by controlling the upregulation of membrane receptors. α- and β spectrins are essential for the development of nervous system.
The spectrin-based membrane skeleton is essential to provide mechanical stability and membrane integrity. It is also responsible for protein organization, trafficking and resilience of erythrocytes.
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