|Detection of Human APLP‑2 by Western Blot. Western blot shows lysates of SH‑SY5Y human neuroblastoma cell line. PVDF Membrane was probed with 1 µg/mL of Human APLP‑2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF4945) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for APLP‑2 at approximately 115 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
APLP-2 is a 100-170 kDa glycoprotein, member of the APP family of neuronal type I transmembrane proteins. Its extracellular domain consists of an N-terminal Cys-rich domain, an Asp/Glu-rich acidic region, a Kunitz protease inhibitor (KPI) domain, and a GAG attachment site in the membrane proximal domain. APLP-2 forms both homodimers and heterodimers with APP and APLP-1. Proteolytic cleavage of APLP-2 generates peptides similar to the amyloidogenic A beta peptides and a cytoplasmic fragment that functions as a transcriptional coactivator. Alternate splicing of APLP-2 generates isoforms that lack the KPI domain or contain an insertion that prevents GAG attachment. The extracellular domain of human APLP-2 shares 81% and 93% amino acid sequence identity with mouse and rat APLP-2, respectively.
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