Recombinant Human Tenascin C Protein, CF

Catalog # Availability Size / Price Qty
3358-TC-050
Product Details
Citations (8)
FAQs
Supplemental Products
Reviews (1)

Recombinant Human Tenascin C Protein, CF Summary

Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by the ability of the immobilized protein to block Fibronectin-mediated adhesion of NIH‑3T3 mouse embryonic fibroblast cells. rhTenascin-C immobilized at 15 μg/mL, in the presence of 0.1 μg/mL human Fibronectin, will block approximately 70%-90% NIH3/T3 cell adhesion (5 x 104 cells/well, 100 μL/well).
Source
Mouse myeloma cell line, NS0-derived human Tenascin C protein
Gly23-Pro625, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Analysis
Gly23
Predicted Molecular Mass
65.3 kDa
SDS-PAGE
97 kDa, reducing conditions

Product Datasheets

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

3358-TC

Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 500 μg/mL in sterile PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
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.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
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Reconstitution Calculator

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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 (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.

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

Citations for Recombinant Human Tenascin C Protein, CF

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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  1. Microenvironmental Factors Drive Tenascin C and Src Cooperation to Promote Invadopodia Formation in Ewing Sarcoma
    Authors: AG Hawkins, CM Julian, S Konzen, S Treichel, ER Lawlor, KM Bailey
    Neoplasia, 2019;21(10):1063-1072.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Targeted disruption of the iNOS gene improves adipose tissue inflammation and fibrosis in leptin-deficient ob/ob mice: role of tenascin C
    Authors: S Becerril, A Rodríguez, V Catalán, L Méndez-Gim, B Ramírez, N Sáinz, M Llorente, X Unamuno, J Gómez-Ambr, G Frühbeck
    Int J Obes (Lond), 2018;0(0):.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Acetyl-CoA promotes glioblastoma cell adhesion and migration through Ca2+-NFAT signaling
    Authors: JV Lee, CT Berry, K Kim, P Sen, T Kim, A Carrer, S Trefely, S Zhao, S Fernandez, LE Barney, AD Schwartz, SR Peyton, NW Snyder, SL Berger, BD Freedman, KE Wellen
    Genes Dev., 2018;32(7):497-511.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  4. Activation of NOTCH signaling by tenascin-C promotes growth of human brain tumor-initiating cells
    Authors: S Sarkar, R Mirzaei, FJ Zemp, W Wu, DL Senger, SM Robbins, VW Yong
    Cancer Res., 2017;0(0):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  5. Integrins functioning in uterine endometrial stromal and epithelial cells in estrus
    Authors: Hye Jin Park
    Reproduction, 2016;0(0):.
    Applications: Bioassay
  6. Migration of breast cancer cell lines in response to pulmonary laminin 332
    Cancer Med, 2016;0(0):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  7. 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 Types: Whole Cells
    Applications: Bioassay
  8. Extracellular matrix protein tenascin-C is required in the bone marrow microenvironment primed for hematopoietic regeneration.
    Authors: Nakamura-Ishizu A, Okuno Y, Omatsu Y, Okabe K, Morimoto J, Uede T, Nagasawa T, Suda T, Kubota Y
    Blood, 2012;119(23):5429-37.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay

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Recombinant Human Tenascin C Protein, CF
By Anonymous on 03/12/2019
Application: IT WORKS WELL FOR GROWING CELLS.