Human Tenascin R Antibody

Catalog # Availability Size / Price Qty
Tenascin R in Human Brainstem.
1 Image
Product Details
Citations (11)
Supplemental Products

Human Tenascin R Antibody Summary

Species Reactivity
Detects human Tenascin R in direct ELISAs and Western blots. In direct ELISAs and Western blots, less than 1% cross-reactivity with recombinant human Tenascin C is observed.
Polyclonal Goat IgG
Antigen Affinity-purified
Mouse myeloma cell line NS0-derived recombinant human Tenascin R isoform 1
Accession # Q92752
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.


Recommended Concentration
Western Blot
0.1 µg/mL
Recombinant Human Tenascin R (Catalog # 3865-TR)
5-15 µg/mL
See below

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.

Scientific Data

Immunohistochemistry Tenascin R antibody in Human Brainstem by Immunohistochemistry (IHC-P). View Larger

Tenascin R in Human Brainstem. Tenascin R was detected in immersion fixed paraffin-embedded sections of human brainstem (medulla) using 1.7 µg/mL Goat Anti-Human Tenascin R Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3865) overnight at 4 °C. Tissue was stained with the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.

Reconstitution Calculator

Reconstitution Calculator

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Preparation and Storage

Reconstitute at 0.2 mg/mL in sterile PBS.
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 R

Tenascin R (TNR) is an extracellular matrix glycoprotein belonging to the tenascin family of adhesion proteins (1-3). TNR is expressed in the central nervous system by oligodendrocytes and selected inhibitory interneurons. It shows highest expression during the postnatal period of active myelination and promotes neurite outgrowth and synaptic functions (1, 2). It is essential for formation of perineuronal nets, the mesh-like network of extracellular matrix (ECM) molecules that surrounds some neurons (4). The 180 kDa, 1327 amino acid (aa) form of human TNR contains a signal sequence, three heptad repeats that mediate coiled-coil trimer formation, five EGF-like repeats, nine fibronectin type III repeats (FN), and a C-terminal Ca2+-binding fibrinogen-related domain. TNR isoform 2 (160 kDa) lacks a portion of FN#6 (aa 773-862) (3). Mature human TNR isoform 1 shows 94%, 94%, 93%, 93%, and 76% aa identity with bovine, mouse, rat, canine, and chicken TNR, respectively. Experiments using recombinant TNR fragments indicate that EGF-like domains are counteradhesive for neurons and microglia and contribute to their migration (1, 5-7). This region interacts with immunoglobulin superfamily molecules including contactin, phosphacan and voltage-gated sodium channel beta subunits. However, the fibronectin domains are adhesive for the lectican family of chondroitin sulfate proteoglycans (brevican, aggrican, versican and neurocan; FN 3-5), contactin (FN 2-3) and sodium channel beta subunits (FN 6-8) (6-9). These adhesive interactions can compete with each other, but can also contribute to crosslinking of lecticans and contactin with other ECM molecules to form perineuronal nets (9, 10). Post-translational modification of TNR can differ with time and location (11). Notably, glycosylation may include GalNAc-4-SO4, O-linked sialylated glycans, “brain-type” neutral N-glycans and the HNK-1 carbohydrate epitope that is thought to be involved in regulation of synaptic plasticity (11, 12).

  1. Jones, F.S. and P.L. Jones (2000) Dev. Dyn. 218:235.
  2. Dityatev, A. and M. Schachner (2006) Cell Tissue Res. 326:647.
  3. Carnemolla, B. et al. (1996) J. Biol. Chem. 271: 8157.
  4. Weber, P. et al. (1999) J. Neurosci. 19:4245.
  5. Xiao, Z.C. et al. (1997) J. Neurosci. Res. 49:698.
  6. Xiao, Z.C. et al. (1999) J. Biol. Chem. 274:26511.
  7. Liao, H. et al. (2005) J. Biol. Chem. 280:8316.
  8. Aspberg, A. et al. (1997) Proc. Natl. Acad. Sci. USA 94:10116.
  9. Lundell, A. et al. (2004) Structure 12:1495.
  10. Zacharias, U. and U. Rauch (2006) J. Cell Sci. 119:3456.
  11. Woodworth, A. et al. (2004) J. Biol. Chem. 279:10413.
  12. Zamze, S. et al. (1999) Glycobiology 9:823.
Entrez Gene IDs
7143 (Human); 21960 (Mouse); 25567 (Rat)
Alternate Names
Janusin; MGC149328; Restrictin; tenascin R (restrictin, janusin); Tenascin R; tenascin-R; TNR; TN-R

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Citations for Human Tenascin R Antibody

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.

11 Citations: Showing 1 - 10
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  1. Reduced length of nodes of Ranvier and altered proteoglycan immunoreactivity in prefrontal white matter in major depressive disorder and chronically stressed rats
    Authors: José Javier Miguel-Hidalgo, Erik Hearn, Mohadetheh Moulana, Khunsa Saleem, Austin Clark, Maggie Holmes et al.
    Sci Rep
  2. Component-specific reduction in perineuronal nets in senescence-accelerated mouse strains
    Authors: Hiroshi Ueno, Yu Takahashi, Shinji Murakami, Kenta Wani, Tetsuji Miyazaki, Yosuke Matsumoto et al.
    IBRO Neuroscience Reports
  3. Integrative multiomic analyses of dorsal root ganglia in diabetic neuropathic pain using proteomics, phospho-proteomics, and metabolomics
    Authors: M Doty, S Yun, Y Wang, M Hu, M Cassidy, B Hall, AB Kulkarni
    Scientific Reports, 2022-10-11;12(1):17012.
    Species: Human
    Sample Types: Cell Culture Supernates, Whole Tissue
    Applications: IHC, Western Blot
  4. CAQK, a peptide associating with extracellular matrix components targets sites of demyelinating injuries
    Authors: Charly Abi-Ghanem, Deepa Jonnalagadda, Jerold Chun, Yasuyuki Kihara, Barbara Ranscht
    Frontiers in Cellular Neuroscience
  5. Assessment of Possible Contributions of Hyaluronan and Proteoglycan Binding Link Protein 4 to Differential Perineuronal Net Formation at the Calyx of Held
    Authors: Kojiro Nojima, Haruko Miyazaki, Tetsuya Hori, Lydia Vargova, Toshitaka Oohashi
    Frontiers in Cell and Developmental Biology
  6. Distribution and classification of the extracellular matrix in the olfactory bulb
    Authors: Andrea Hunyadi, Botond Gaál, Clara Matesz, Zoltan Meszar, Markus Morawski, Katja Reimann et al.
    Brain Structure and Function
  7. Layer-specific expression of extracellular matrix molecules in the mouse somatosensory and piriform cortices
    Authors: H Ueno, S Suemitsu, S Murakami, N Kitamura, K Wani, Y Matsumoto, M Okamoto, T Ishihara
    IBRO Rep, 2018-11-28;6(0):1-17.
    Species: Mouse
    Sample Types: Whole Tissue
    Applications: IHC-Fr
  8. Sensory experience-dependent formation of perineuronal nets and expression of Cat-315 immunoreactive components in the mouse somatosensory cortex
    Authors: H Ueno, S Suemitsu, M Okamoto, Y Matsumoto, T Ishihara
    Neuroscience, 2017-05-08;0(0):.
    Species: Mouse
    Sample Types: Whole Tissue
    Applications: IHC-Fr
  9. A peptide for targeted, systemic delivery of imaging and therapeutic compounds into acute brain injuries
    Authors: Aman P. Mann, Pablo Scodeller, Sazid Hussain, Jinmyoung Joo, Ester Kwon, Gary B. Braun et al.
    Nature Communications
  10. Extracellular matrix protein expression is brain region dependent
    Authors: Stephanie Dauth, Thomas Grevesse, Harry Pantazopoulos, Patrick H. Campbell, Ben M. Maoz, Sabina Berretta et al.
    Journal of Comparative Neurology
  11. Extracellular matrix molecules exhibit unique expression pattern in the climbing fiber-generating precerebellar nucleus, the inferior olive.
    Authors: Kecskes S, Gaal B, Racz E, Birinyi A, Hunyadi A, Matesz C
    Neuroscience, 2014-10-17;284(0):412-21.
    Species: Rat
    Sample Types: Whole Tissue
    Applications: IHC


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