|Detection of Rat Teneurin‑4 by Western Blot. Western blot shows lysates of rat embryonic cortical neurons. PVDF membrane was probed with 1 µg/mL of Sheep Anti-Human/Mouse/Rat Teneurin‑4 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF6320) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for Teneurin‑4 at approximately 250 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8.|
Teneurin-4 (also Ten-m4, Doc4 and tenascin-M4) is a 250-300 kDa member of the tenascin family, teneurin subfamily of transmembrane (TM) molecules. It is a covalently-linked homodimer that is widely expressed in the embryo, and in adult, participates in cell-to-cell adhesion, and may communicate ER stress levels. Human Teneurin-4 is a 2769 amino acid (aa) type II TM glycoprotein. It contains a 345 aa cytoplasmic region (aa 1-345), plus a 2403 aa extracellular domain (ECD) (aa 367‑2769). The ECD possesses eight sequential EGF-like domains (aa 561-831), five NHL repeats, each of which form a beta -propeller (aa 1216-1566), and 23 YD/TyrAsp-containing repeats that bind carbohydrates. C-terminal cleavage generates a short 5 kDa, 41 aa peptide (aa 2726-2766) termed TCAP-1 that shows bioactivity. Teneurin-4 is hypothesized to form heterodimers with other teneurins. Over aa 61-340, human Teneurin-4 shares 95% aa identity with mouse Teneurin-4.
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