抗Tenascin C抗体(Anti-Tenascin C, Mouse, Rat-Mono antibody)

• 価格
• Product Details
• Applications and Data
• Related Product & Information
• Citations

価格

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Product Details

Species Reactivity	Human, Mouse
Label	Unconjugated
Immunogen	Mouse immature astrocyte-derived Tenascin C
Source	Monoclonal Rat IgG2A Clone # 578
Purification	Protein A or G purified from hybridoma culture supernatant
Specificity	Detect human and mouse Tenascin C in Western blots.

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Applications and Data

	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.

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.

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Related Product & Information

Entrez Gene IDs	3371 (Human); 21923 (Mouse); 116640 (Rat)
Background	Tenascin C
background_content	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 by15 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.

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Citations

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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