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Collagens are the most abundant proteins in the extracellular matrix (ECM). In fact collagens are the most abundant proteins in the human body. Collagens, as fibers, form the extracellular part of tissue that provides structural support and fulfills numerous cellular functions for animal cells. The ECM is the defining feature of connective tissue in animals and includes the interstitial matrix and the basement membrane. Interstitial matrix present between various animal cells serves as a compression buffer against the stress placed on the ECM. Basement membranes are sheet-like depositions of ECM on which various epithelial cells rest.
Fibronectin, laminin and elastin are other major components of the ECM that provide for movement, tensile resistance and elasticity, respectively. These proteins are representative of the diverse composition of the ECM and serve many functions, including providing support, segregating tissues from one another, and regulating intercellular communication. The ECM regulates a cell's dynamic behavior and sequesters a wide range of cellular growth factors.
Formation of the extracellular matrix is essential for processes like growth, wound healing and fibrosis. This makes studying the ECM crucial for medical applications and further research innovations such as tissue engineering. It can also help in comprehending the complex dynamics of tumor invasion and metastasis in cancer biology.
Immunization with type II collagen within complete Freund's adjuvant leads to Arthritis. Injection of anti-tumor necrosis factor (TNF) IgG, after immunization prevented the development of arthritis1. Extracellular matrix (ECM) proteins are produced intracellularly and are subsequently secreted into the surrounding cellular medium, actively regulating a diverse range of cell functions including cell adhesion, differentiation and survival. A primary utility of ECMs in in vitro culture is to promote cellular adhesion while maintaining cell viability and maximizing cell proliferation for downstream cell-based applications. Rockland provides a wide variety of Collagen proteins for your research needs. Rockland’s 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 Collagen proteins are negligible (typically less than 1% cross reactivity was detected by ELISA). Additionally, we offer our collagen proteins in frozen sections or paraffin (protease) to fit your research needs. Frozen sections tend to preserve antigenic content better, while paraffin blocks provide better morphology and the ability to use larger pieces of tissue.
Extracellular matrix proteins and antibodies that are conjugated for specific reactions within the ECM can help researchers understand how cancer and other diseases function on a cellular level. This provides valuable insight into the molecular processes that drive disease and points to methods of mitigating or curing them.
While the packing structure of collagen has not been completely defined, it has been long known to be hexagonal or quasi-hexagonal. Various cross linking agents like dopaquinone, embelin, potassium embelate and 5-O-methyl embelin could be developed as potential cross-linking/stabilization agents of collagen preparation and its application are enhanced. Additionally, collagen is a composed of a triple helix, of amino acids that is atypical for proteins, particularly with respect to its high hydroxyproline content. The most common motifs in the amino acid sequence of collagen are Glycine-Proline-X and Glycine-X-Hydroxyproline, where X is any amino acid other than glycine, proline or hydroxyproline.
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 keratin. 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.
Extracellular matrix cells can cause regrowth and healing of tissue, working with stem cells in human fetuses to grow and regrow all parts of the human body (fetuses can regrow anything that gets damaged in the womb). The ECM serves two main purposes in tissue healing: it prevents the immune system from triggering from the injury and responding with inflammation and scar tissue and it facilitates the surrounding cells to repair the tissue instead of forming scar tissue.
As of early 2007, testing was being carried out on a military base in Texas with scientists using a powdered form on Iraq War veterans whose hands were damaged in the war.
Extracellular matrix proteins are commonly used in cell culture systems to maintain stem and precursor cells in an undifferentiated state during cell culture and function to induce differentiation of epithelial, endothelial and smooth muscle cells in vitro. Extracellular matrix proteins can also be used to support 3D cell culture in vitro for modeling tumor development.
Rockland Immunochemicals Inc.Limerick, PA 19468E-mail: firstname.lastname@example.orgPhone: 800.656.7625