The extracellular matrix (ECM) is the external framework found between individual cells that comprise higher order structures like tissues and organs. The ECM composition of vertebrates is dominated by a class of molecules known as collagens - each with unique features suited for a particular function and location. Collagen proteins are made up of three subunit polypeptides that vary in length. Through a unique repeated (Gly-X-Y) sequence, these components associate to form a structurally regular triple helix. Collagen type I is one of the most common collagen forms and is found in a wide variety of areas including skin, tendon, vascular ligature, organs, and bone. Because of collagen I’s basic and fundamental role in guiding ECM architecture, its identification and detection is useful in the classification and verification of tissue-specific origins, and sample tissue typing.
Collagen I antibody was used by Hashimoto’s group from the University of Michigan to establish that collagen-producing lung fibroblasts in pulmonary fibrosis actually derive from bone marrow (BM) progenitor cells1. Gilkes et al examined the transcriptional regulation of procollagen lysyl hydroxylase 2 (PLOD2) and hypoxia-inducible Factor 1 (HIF-1) in breast cancer metastasis 2. Their data relied upon the Collagen I antibody to validate the role of PLOD2 in fibrillar collagen formation, tumor structural stiffness, and metastasis formation. Follow-up studies used the Collagen I antibody to monitor HIF-1-dependent ECM remodeling in the same breast cancer system3. The Collagen I antibody was used to develop a rapid and efficient means of studying the differentiation murine spleen cells under serum-free culturing conditions4. Immunohistochemistry with the Collagen I antibody also allowed Triulzi’s group to assess collagen-related microenvironment modifications that are triggered by maspin, a serpin protease inhibitor5.
Novus Biologicals offers Collagen I reagents for your research needs including:
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