Recombinant Human Tenascin C Protein, CF

Tenascin C, also known as hexabrachion, cytotactin, neuronectin, GMEM, JI, myotendinous antigen, glioma-associated-extracellular matrix antigen, and GP 150-225, is a member of the Tenascin family of extracellular matrix proteins. It is secreted as a disulfide-linked homohexamer whose subunits can vary in size from approximately 200 kDa to over 300 kDa due to differences in glycosylation (1). Rotary-shadowed electron micrographs of the purified molecule show six strands joined to one another at one end in a globular domain with each arm terminating in a knob-like structure (2-3). The human Tenascin C monomer is synthesized as a precursor with a 22 amino acid (aa) signal sequence and a 2179 aa mature chain (SwissProt # P24821). The mature chain consists of a coiled-coil region (aa 118-145), followed by 15 EGF-like domains, 15 fibronectin type-III domains, and a fibrinogen C-terminal domain. In addition, there are 23 potential sites of N-linked glycosylation. Alternative splicing within the fibronectin type-III repeats produces six isoforms for human Tenascin C. Mature human Tenascin C (isoform 1) shares 84% aa sequence identity with mature mouse Tenascin C. In the developing embryo, Tenascin C is expressed during neural, skeletal, and vascular morphogenesis (1, 2). In the adult, it virtually disappears with continued basal expression detectable only in tendon-associated tissues (1, 2). However, greatup-regulation in expression occurs in tissues undergoing remodeling processes seen during wound repair and neovascularization or in pathological states such as inflammation or tumorigenesis (1, 4-5). Biologically, Tenascin C functions as an adhesion-modulatory extracellular matrix protein (1, 4-8). Specifically, it antagonizes the adhesive effects of fibronectin, and impacts the ability of fibroblasts to deposit and contract the matrix by affecting the morphology and signaling pathways of adherent cells (5-7). Tenascin C acts by blocking syndecan-4 binding at the edges of the wound and by suppressing fibronectin-mediated activation of RhoA and focal adhesion kinase (FAK) (4-8). Tenascin C thus promotes epidermal cell migration and proliferation during wound repair.

• Tenascin C Antibodies
• Tenascin C ELISA Kits
• Tenascin C Protein
• Tenascin C Proteins and Enzyme