|Detection of Human FABP8/M‑FABP by Western Blot Western blot shows lysates of human brain (cerebellum) tissue. PVDF Membrane was probed with 2 µg/mL of Mouse Anti-Human FABP8/M‑FABP Monoclonal Antibody (Catalog # MAB5866) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band was detected for FABP8/M‑FABP at approximately 15 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
FABP8/M‑FABP in Human Spinal Cord.|
FABP8/M‑FABP was detected in immersion fixed paraffin-embedded sections of human spinal cord using using Mouse Anti-Human FABP8/
M‑FABP Monoclonal Antibody (Catalog # MAB5866) at 15 µg/mL overnight at 4 °C. Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using Antigen Retrieval Reagent-Basic (Catalog # CTS013). Tissue was stained using the Anti-Mouse HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS002) and counterstained with hematoxylin (blue). Specific staining was localized to white matter. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.
FABP8 (fatty acid binding protein-8; also M [myelin]-FABP, P2 and PMP2) is a 15 kDa (predicted) member of the fatty acid binding protein family, calycin superfamily of molecules. It is found in Schwann cells, presumably on the cytoplasmic face of the plasma membrane where it may contribute to fatty acid transport across myelin. Functionally, FABP8 has a high affinity for U-shaped fatty acids such as oleic and palmitic acid. Human FABP8 is 132 amino acids (aa) in length and exhibits two layers of antiparallel beta -strands that envelope a hydrophobic pocket for lipid binding. Arg107 plus Arg127-Ile128-Tyr129 participate in fatty acid binding. Full length human FABP8 shares 87% and 95% aa identity with mouse and rabbit FABP9, respectively.