Extracellular Matrix Combinatorial Library Launched

30 Oct 2012
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AMSBIO is a leading supplier of innovative tools for growing cells in a physiologically relevant manner. A unique Extracellular Matrix (ECM) Mimetic Library for engineering surfaces to direct receptor binding specificity, signaling and growing cells in 3D has been launched.

Containing nearly 300 biomimetics of Fibronectin, Vitronectin, Laminin and Collagen, for coating plates or creating 3D culture scaffolds, AMSBIO's new ECM combinatorial library provides a powerful tool for identifying the cellular adhesion profile of your cell line or tumor against the widest commercially available collection of cell surface receptor binding peptide motifs.

The extracellular microenvironment, defined by biochemical and physical cues, is a deciding factor in a wide range of cellular processes not confined solely to oncology. These include cell adhesion, proliferation, differentiation, and expression of phenotype-specific functions. Being able to engineer the ECM microenvironment provides clear benefits in studies of cell and tissue engineering and related applications. Currently existing technology offers simple (and merely adequate) environments that facilitate basic cell processes such as adhesion. The simple presentation of motifs involved in cell adhesion is not optimal for controlling more integrated processes. Crosstalk among signaling pathways acts synergistically to enhance cellular responses such as cell adhesion and/or proliferation.

A recent study showed that a combination of extracellular matrix derived peptides presented on a surface may enhance cell adhesion strength and focal adhesion assembly. This combinatorial presentation of ECM peptides on cell growth surfaces may also promote elevated proliferation rates of primary or stem cells.

Based upon the AMSBIO ECM combinatorial library, the ready to-use MAPTrix™ Array provides a means to regulate a variety of cell surface receptors for your cell studies. The basic layout of the MAPTrix™ Array is comprised of avß3 and its complementary integrins such as a2ß1 (collagen), a3ß1 (laminin), a5ß1 (fibronectin), and heparin binding motif.

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