Human Tenascin C Biotinylated Antibody Summary
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
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Preparation and Storage
- 12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 6 months, -20 to -70 degreesC under sterile conditions after reconstitution.
Background: Tenascin C
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. 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, great up-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.
- Hsia, H.C. and J.E. Schwarzbauer (2005) J. Biol. Chem. 280:26641.
- Nies, D.E. et al. (1991) J. Biol. Chem. 266:2818.
- Erickson, H.P and J.L. Iglesias (1984) Nature 311:267.
- Orend, G. et al. (2003) Oncogene 22:3917.
- Wenk, M.B. et al. (2000) J. Cell Biol. 150:913.
- Midwood, K.S. et al. (2004) Mol. Biol. Cell 15:5670.
- Midwood, K.S. and J. E. Schwarzbauer (2002) Mol. Biol. Cell 13:3601.
- Hsia, H.C. and J.E. Schwarzbauer (2006) J. Surg. Res. 136:92.
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