This recombinant mouse Tenascin-R (Tnr) is a semi-custom product. There are 5 expression system options: Yeast, E. coli, In Vivo Biotinylation in E. coli, Baculovirus, and Mammalian cell. Your requirements will be given top priority in determining the protein tags. For proteins within 800 aa, risk-free custom service is guaranteed. It means you will not be charged if the protein cannot be delivered.
Tnr is an extracellular matrix glycoprotein that plays a crucial role in various processes within the nervous system, including neurite outgrowth, neural cell adhesion, proliferation, migration, axonal guidance, myelination, and synaptic plasticity [1]. Unlike tenascin-C (Tnc), which is also found in non-nervous tissues, Tnr is expressed exclusively in the nervous system [2]. Studies have shown that Tnr is expressed by oligodendrocytes and certain neuronal subpopulations in the central nervous system of vertebrates [3]. Furthermore, Tnr has been found to prevent the formation of myelin membranes and regulate the expression of myelin basic protein [4].
Research has indicated that Tnr can restrict posttraumatic remodeling of motoneuron innervation and hinder functional recovery after spinal cord injury in adult mice [3]. Additionally, Tnr participates in the extracellular matrix formation and stabilization of perineuronal nets by clustering aggrecan [5]. Moreover, Tnr has been shown to interfere with remyelination processes in models of demyelination, indicating its role in myelin regeneration [6][7]. Evidence showed that Tnr is linked to synaptic plasticity and maintains a balance between excitatory and inhibitory circuits involved in learning, memory, and cognition [8].
References:
[1] M. Wagner, J. Lévy, S. Jung-Klawitter, S. Bakhtiari, F. Monteiro, R. Maroofianet al., Loss of Tnr causes a nonprogressive neurodevelopmental disorder with spasticity and transient opisthotonus, Genetics in Medicine, vol. 22, no. 6, p. 1061-1068, 2020. https://doi.org/10.1038/s41436-020-0768-7
[2] J. Reinhard, L. Roll, & A. Faissner, Tenascins in retinal and optic nerve neurodegeneration, Frontiers in Integrative Neuroscience, vol. 11, 2017. https://doi.org/10.3389/fnint.2017.00030
[3] I. Apostolova, A. Irintchev, & M. Schachner, Tenascin-r restricts posttraumatic remodeling of motoneuron innervation and functional recovery after spinal cord injury in adult mice, Journal of Neuroscience, vol. 26, no. 30, p. 7849-7859, 2006. https://doi.org/10.1523/jneurosci.1526-06.2006
[4] T. Czopka, A. Holst, G. Schmidt, C. ffrench‐Constant, & A. Faissner, Tenascin c and tenascin r similarly prevent the formation of myelin membranes in a rhoa‐dependent manner, but antagonistically regulate the expression of myelin basic protein via a separate pathway, Glia, vol. 57, no. 16, p. 1790-1801, 2009. https://doi.org/10.1002/glia.20891
[5] M. Morawski, A. Dityatev, M. Hartlage‐Rübsamen, M. Blosa, M. Holzer, K. Flachet al., Tenascin-r promotes assembly of the extracellular matrix of perineuronal nets via clustering of aggrecan, Philosophical Transactions of the Royal Society B Biological Sciences, vol. 369, no. 1654, p. 20140046, 2014. https://doi.org/10.1098/rstb.2014.0046
[6] J. Bauch and A. Faissner, The extracellular matrix proteins tenascin-c and tenascin-r retard oligodendrocyte precursor maturation and myelin regeneration in a cuprizone-induced long-term demyelination animal model, Cells, vol. 11, no. 11, p. 1773, 2022. https://doi.org/10.3390/cells11111773
[7] J. Bauch, S. Ort, A. Ulc, & A. Faissner, Tenascins interfere with remyelination in an ex vivo cerebellar explant model of demyelination, Frontiers in Cell and Developmental Biology, vol. 10, 2022. https://doi.org/10.3389/fcell.2022.819967
[8] D. Dufresne, F. Hamdan, J. Rosenfeld, B. Torchia, B. Rosenblatt, J. Michaudet al., Homozygous deletion of tenascin-r in a patient with intellectual disability, Journal of Medical Genetics, vol. 49, no. 7, p. 451-454, 2012. https://doi.org/10.1136/jmedgenet-2012-100831
