Human/Mouse Tenascin C Antibody

(8 citations)   
  • Species Reactivity
    Human, Mouse
  • Specificity
    Detect human and mouse Tenascin C in Western blots.
  • Source
    Monoclonal Rat IgG2A Clone # 578
  • Purification
    Protein A or G purified from hybridoma culture supernatant
  • Immunogen
    Mouse immature astrocyte-derived Tenascin C
  • Formulation
    Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
  • Endotoxin Level
    <0.10 EU per 1 μg of the antibody by the LAL method.
  • Label
    Unconjugated
Applications
  •  
    Recommended
    Concentration
    Sample
  • Western Blot
    Morganti, M. et al. (1990) Exp. Neurol. 109:98.
  • Immunocytochemistry
    8-25 µg/mL
    See below
  • Neutralization
    Husmann, K. et al. (1992) J. Cell Biol. 116:1475.
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.
Data Examples
Immunocytochemistry
Tenascin C in U‑118 MG Human Cell Line.

Tenascin C was detected in immersion fixed U‑118 MG human glioblastoma/astrocytoma cell line using Rat Anti-Human/Mouse Tenascin C Monoclonal Antibody (Catalog # MAB2138) at 10 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Rat IgG Secondary Antibody (yellow; Catalog # NL013) and counterstained with DAPI (blue). View our protocol for Fluorescent ICC Staining of Cells on Coverslips.

Preparation and Storage
  • Reconstitution
    Reconstitute at 0.5 mg/mL in sterile PBS.
  • Shipping
    The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
  • Stability & Storage
    Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
    • 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.

  • References:
    1. Hsia, H.C. and J.E. Schwarzbauer (2005) J. Biol. Chem. 280:26641.
    2. Nies, D.E. et al. (1991) J. Biol. Chem. 266:2818.
    3. Erickson, H.P and J.L. Iglesias (1984) Nature 311:267.
    4. Orend, G. et al. (2003) Oncogene 22:3917.
    5. Wenk, M.B. et al. (2000) J. Cell Biol. 150:913.
    6. Midwood, K.S. et al. (2004) Mol. Biol. Cell 15:5670.
    7. Midwood, K.S. and J. E. Schwarzbauer (2002) Mol. Biol. Cell 13:3601.
    8. Hsia, H.C. and J.E. Schwarzbauer (2006) J. Surg. Res. 136:92.
  • Entrez Gene IDs:
    3371 (Human); 21923 (Mouse); 116640 (Rat)
  • Alternate Names:
    150-225; Cytotactin; Glioma-associated-extracellular matrix antigen; GMEM; GP 150-225; hexabrachion (tenascin C, cytotactin); hexabrachion (tenascin); Hexabrachion; HXB; HXBcytotactin; JI; MGC167029; Myotendinous antigen; neuronectin; Tenascin C; Tenascin J1; tenascin; tenascin-C isoform 14/AD1/16; Tenascin-C; TNC; TN-C; TNGP
Related Research Areas
Citations:

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

8 Citations: Showing 1 - 8
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Species
Applications
Sample Type
  1. Combined CSL and p53 downregulation promotes cancer-associated fibroblast activation.
    Authors: Procopio M, Laszlo C, Al Labban D, Kim D, Bordignon P, Jo S, Goruppi S, Menietti E, Ostano P, Ala U, Provero P, Hoetzenecker W, Neel V, Kilarski W, Swartz M, Brisken C, Lefort K, Dotto G
    Nat Cell Biol, 2015;17(9):1193-204.
    Species: Mouse
    Sample Type: Whole Tissue
    Application: IHC - Not specified
  2. Temporal expression of growth factors triggered by epiregulin regulates inflammation development.
    Authors: Harada M, Kamimura D, Arima Y, Kohsaka H, Nakatsuji Y, Nishida M, Atsumi T, Meng J, Bando H, Singh R, Sabharwal L, Jiang J, Kumai N, Miyasaka N, Sakoda S, Yamauchi-Takihara K, Ogura H, Hirano T, Murakami M
    J Immunol, 2015;194(3):1039-46.
    Species: Mouse
    Sample Type: In Vivo
    Application: In vivo
  3. The missense mutation p.R1303Q in type XVII collagen underlies junctional epidermolysis bullosa resembling Kindler syndrome.
    Authors: Has, Cristina, Kiritsi, Dimitra, Mellerio, Jemima E, Franzke, Claus-We, Wedgeworth, Emma, Tantcheva-Poor, Iliana, Kernland-Lang, Kristin, Itin, Peter, Simpson, Michael, Dopping-Hepenstal, Patricia, Fujimoto, Wataru, McGrath, John A, Bruckner-Tuderman, Leena
    J Invest Dermatol, 2014;134(3):845-9.
    Species: Human
    Sample Type: Whole Tissue
    Application: IHC - Not specified
  4. Melanoma cell invasiveness is promoted at least in part by the epidermal growth factor-like repeats of tenascin-C.
    Authors: Grahovac, Jelena, Becker, Dorothea, Wells, Alan
    J Invest Dermatol, 2013;133(1):210-20.
    Species: Human
    Sample Type: Cell Lysates
    Application: WB
  5. Mechanisms of fibroblast cell therapy for dystrophic epidermolysis bullosa: high stability of collagen VII favors long-term skin integrity.
    Authors: Kern JS, Loeckermann S, Fritsch A, Hausser I, Roth W, Magin TM, Mack C, Muller ML, Paul O, Ruther P, Bruckner-Tuderman L
    Mol. Ther., 2009;17(9):1605-15.
    Species: Mouse
    Sample Type: Whole Tissue
    Application: IHC
  6. A hypomorphic mouse model of dystrophic epidermolysis bullosa reveals mechanisms of disease and response to fibroblast therapy.
    Authors: Fritsch A, Loeckermann S, Kern JS, Braun A, Bosl MR, Bley TA, Schumann H, von Elverfeldt D, Paul D, Erlacher M, Berens von Rautenfeld D, Hausser I, Fassler R, Bruckner-Tuderman L
    J. Clin. Invest., 2008;118(5):1669-79.
    Species: Mouse
    Sample Type: Whole Tissue
    Application: IHC Frozen
  7. ELR-negative CXC chemokine CXCL11 (IP-9/I-TAC) facilitates dermal and epidermal maturation during wound repair.
    Authors: Yates CC, Whaley D, Y-Chen A, Kulesekaran P, Hebda PA, Wells A
    Am. J. Pathol., 2008;173(3):643-52.
    Species: Mouse
    Sample Type: Whole Tissue
    Application: IHC Paraffin-embedded
  8. Essential role of Smad3 in infarct healing and in the pathogenesis of cardiac remodeling.
    Authors: Bujak M, Ren G, Kweon HJ, Dobaczewski M, Reddy A, Taffet G, Wang XF, Frangogiannis NG
    Circulation, 2007;116(19):2127-38.
    Species: Mouse
    Sample Type: Whole Tissue
    Application: IHC Paraffin-embedded
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