Human APP (Amyloid Precursor Protein) CLIA Kit

Amyloid-Beta Precursor Protein; App; Abpp; Appi; Alzheimer Disease Amyloid Protein; Amyloid Precursor Protein; Amyloid-Beta A4 Protein; Cerebral Vascular Amyloid Peptide; Cvap; Prea4; Protease Nexin-Ii; Pn-Ii Cleaved Into - N-App - Soluble App-Alpha; S-App-Alpha - Soluble App-Beta; S-App-Beta - C99; Beta-Secretase C-Terminal Fragment; Beta-Ctf - Amyloid-Beta Protein 42; Abeta42; Beta-App42 - Amyloid-Beta Protein 40; Abeta40; Beta-App40 - C83; Alpha-Secretase C-Terminal Fragment; Alpha-Ctf - P3(42 - P3(40 - C80 - Gamma-Secretase C-Terminal Fragment 59; Amyloid Intracellular Domain 59; Aicd-59; Aid(59; Gamma-Ctf(59 - Gamma-Secretase C-Terminal Fragment 57; Amyloid Intracellular Domain 57; Aicd-57; Aid(57; Gamma-Ctf(57 - Gamma-Secretase C-Terminal Fragment 50; Amyloid Intracellular Domain 50; Aicd-50; Aid(50; Gamma-Ctf(50 - C31

Uniprot ID: FOXO3_HUMAN ; Reactome: R-HSA-114608 ; Gene ID: 351

Tissue Specificity: Expressed in the brain and in cerebrospinal fluid (at protein level). Expressed in all fetal tissues examined with highest levels in brain, kidney, heart and spleen. Weak expression in liver. In adult brain, highest expression found in the frontal lobe of the cortex and in the anterior perisylvian cortex-opercular gyri. Moderate expression in the cerebellar cortex, the posterior perisylvian cortex-opercular gyri and the temporal associated cortex. Weak expression found in the striate, extra-striate and motor cortices. Expressed in cerebrospinal fluid, and plasma. Isoform APP695 is the predominant form in neuronal tissue, isoform APP751 and isoform APP770 are widely expressed in non-neuronal cells. Isoform APP751 is the most abundant form in T-lymphocytes. Appican is expressed in astrocytes.

Function: Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapes in axons. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1. Amyloid-beta peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), respectively. Amyloid-beta protein 42 is a more effective reductant than amyloid-beta protein 40. Amyloid-beta peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. APP42-beta may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with overexpressed HADH2 leads to oxidative stress and neurotoxicity. Also binds GPC1 in lipid rafts. Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain. The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis. N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).