|Detection of Human CD96 by Western Blot. Western blot shows lysates of human Th2 cells. PVDF membrane was probed with 1 µg/mL of Sheep Anti-Human CD96 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF6199) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for CD96 at approximately 160 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8.|
CD96 (also Tactile) is a 160 kDa member of the Ig-Superfamily. It is expressed on CD4+ and CD8+ T cells, plus NK cells and select B cells. Human CD96 binds to CD155 and presumably participates in NK cell killing of CD155-expressing target cells. Mature human CD96 is a 564 amino acid (aa), type I transmembrane glycoprotein. It contains a 498 aa extracellular region (aa 22-519) that contains three Ig-like domains. The two N-terminal domains are V-type (aa 38-238), while the distal domain is a C-type structure (aa 269-375). There is one isoform that shows a deletion of aa 183-192. This deletion converts the second V-type domain into an I‑like domain, and generates the most common form of CD96. An additional isoform shows the same deletion coupled to a nine aa substitution for aa 410-585. Over aa 1-536, human CD96 shares 59% aa identity with mouse CD96.
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