Abstract
Integrins are an important family of cell-surface receptors that mediate adhesive interactions. These transmembrane glycoproteins are composed of noncovalently associated α- and β-subunit heterodimers. Twelve different α-chains and eight different β-subunits combine to give more than 20 distinct integrins and alternative splicing of the α- and β-chains increases the complexity of their interactions (1). Integrins have been shown to mediate cell adhesion to at least 12 separate matrix components and are also involved in cell-cell contacts via interactions with members of the immunoglobulin and cadherin families (2). Whereas cellular adhesion to specific components of the extracellular matrix (ECM) is an important function of integrin receptors, signals initiated by ligation of these receptors also modulate cell spreading, migration, proliferation, differentiation, and survival (reviewed in refs. 1 and 3). Specific function-blocking anti-integrin antibodies are invaluable tools with which to study the role of these receptors in mediating the effects of ECM on cellular processes.
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© 1999 Humana Press Inc.
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Edwards, G.M., Streuli, C.H. (1999). Preparing a Polyclonal Antibody to Mouse β1 Integrin with Function-Blocking Activity. In: Howlett, A. (eds) Integrin Protocols. Methods in Molecular Biology, vol 129. Humana Press. https://doi.org/10.1385/1-59259-249-X:135
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DOI: https://doi.org/10.1385/1-59259-249-X:135
Publisher Name: Humana Press
Print ISBN: 978-0-89603-569-0
Online ISBN: 978-1-59259-249-4
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