Anti-Tenascin-R TNR Antibody Picoband® Fluoro647 Conjugated

Tenascin-R is a protein that in humans is encoded by the TNR gene. Tenascin-R (TNR) is an extracellular matrix protein expressed primarily in the central nervous system. It is a member of the tenascin (TN) gene family, which includes at least 3 genes in mammals: TNC (or hexabrachion), TNX (TNXB), and TNR. The genes are expressed in distinct tissues at different times during embryonic development and are present in adult tissues. TNR has been detected predominantly in the central nervous system and is localized around motor neurons and on motor axons in the spinal cord, cerebellum, hippocampus, and olfactory bulb. It is suggested that tenascin-R has a role in initiating the detachment of neuroblasts from tangential chains and in initiating radial migration of the cells.

The antibody was purified from rabbit antiserum by affinity-chromatography using phospho peptide. The antibody against non-phospho peptide was removed by chromatography using corresponding non-phospho peptide.

Neural extracellular matrix (ECM) protein involved in interactions with different cells and matrix components. These interactions can influence cellular behavior by either evoking a stable adhesion and differentiation, or repulsion and inhibition of neurite growth. Binding to cell surface gangliosides inhibits RGD-dependent integrin-mediated cell adhesion and results in an inhibition of PTK2/FAK1 (FAK) phosphorylation and cell detachment. Binding to membrane surface sulfatides results in a oligodendrocyte adhesion and differentiation. Interaction with CNTN1 induces a repulsion of neurons and an inhibition of neurite outgrowth. Interacts with SCN2B may play a crucial role in clustering and regulation of activity of sodium channels at nodes of Ranvier. TNR-linked chondroitin sulfate glycosaminoglycans are involved in the interaction with FN1 and mediate inhibition of cell adhesion and neurite outgrowth. The highly regulated addition of sulfated carbohydrate structure may modulate the adhesive properties of TNR over the course of development and during synapse maintenance (By similarity) . .