Human Tenascin R Antibody
Human Tenascin R Antibody Summary
Glu34-Phe1358
Accession # Q92752
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Applications
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
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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.
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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 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).
- Jones, F.S. and P.L. Jones (2000) Dev. Dyn. 218:235.
- Dityatev, A. and M. Schachner (2006) Cell Tissue Res. 326:647.
- Carnemolla, B. et al. (1996) J. Biol. Chem. 271: 8157.
- Weber, P. et al. (1999) J. Neurosci. 19:4245.
- Xiao, Z.C. et al. (1997) J. Neurosci. Res. 49:698.
- Xiao, Z.C. et al. (1999) J. Biol. Chem. 274:26511.
- Liao, H. et al. (2005) J. Biol. Chem. 280:8316.
- Aspberg, A. et al. (1997) Proc. Natl. Acad. Sci. USA 94:10116.
- Lundell, A. et al. (2004) Structure 12:1495.
- Zacharias, U. and U. Rauch (2006) J. Cell Sci. 119:3456.
- Woodworth, A. et al. (2004) J. Biol. Chem. 279:10413.
- Zamze, S. et al. (1999) Glycobiology 9:823.
Product Datasheets
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.
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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;12(1):17012.
Species: Human
Sample Types: Cell Culture Supernates
Applications: Western Blot -
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, 2019;6(0):1-17.
Species: Mouse
Sample Types: Whole Tissue
Applications: IHC-Fr -
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;0(0):.
Species: Mouse
Sample Types: Whole Tissue
Applications: IHC-Fr -
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, 2015;284(0):412-21.
Species: Rat
Sample Types: Whole Tissue
Applications: IHC
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