Human Tenascin C Biotinylated Antibody
Human Tenascin C Biotinylated Antibody Summary
Accession # BAG64930
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.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C 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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