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Rockland provides highly purified type specific collagen proteins derived from several sources for your research needs. Rockland’s type specific purified collagens are chromatographically and immunologically pure. These proteins are free from other collagens, serum proteins and non-collagen extracellular matrix proteins. Reaction with other type anti-collagen antibodies is minimal (i.e. Collagen Type I react strongly with anti-Collagen Type I antibody but will show minimal reactivity with anti-Collagen Type III antibody by way of example). Most popular Collagen Proteins:
At least eleven (11) genetically distinct gene products are collectively referred to as 'collagen types' or other proteins and proteoglycans of the extracellular matrix. In humans, collagens are composed of about twenty (20) unique protein chains that undergo various types of post-translational modifications and are ultimately assembled into a triple helix (see Figure 2 below). This results in great diversity between collagen types. Collagens are highly conserved throughout evolution and are characterized by an uninterrupted "Glycine-X-Y" triplet repeat that is a necessary part of the triple helical structure. For these reasons, generating type specific antibodies to collagens presents unique challenges. It is an absolute requirement to use non-denatured three-dimensional epitopes to develop these type specific antibodies. Rockland extensively purifies collagens for immunization from human and bovine sources by limited pepsin digestion and selective salt precipitation. This maintains the three-dimensional structure of the collagen.
After isolation from rabbit antiserum, these antibodies are repeatedly and exhaustively cross-adsorbed by immunoaffinity purification to produce 'type' specific antibodies that are well suited to detect extracellular matrix proteins in normal and disease state tissues. For instance, anti-Collagen Type I is first purified against immobilized type I collagen and then is passed over immobilized type II collagen repeatedly until no additional antibody is bound. This process is applied successively for all other collagen types rendering the Collagen Type I antibody specific for collagen I with minimal cross reactivity to all other collagen types.
Many cells bind to components of the extracellular matrix, with cell adhesion occurring in two ways; 1) focal adhesions, connecting the ECM to actin filaments of the cell, and 2) hemidesmosomes, connecting the ECM to intermediate filaments such as ke ratin. This cell-to-ECM adhesion is regulated by specific cell surface cellular adhesion molecules (CAM) known as integrins. Fibronectins bind to ECM macromolecules and facilitate their binding to transmembrane integrins, initiating intracellular signaling pathways as well as association with the cellular cytoskeleton via a set of adaptor molecules.
Rockland Immunochemicals Inc.Limerick, PA 19468E-mail: firstname.lastname@example.orgPhone: 800.656.7625