Background: This gene encodes a cell surface receptor and transmembrane precursor protein that is cleaved by secretases to form a number of peptides. Some of these peptides are secreted and can bind to the acetyltransferase complex APBB1/TIP60 to promote transcriptional activation, while others form the protein basis of the amyloid plaques found in the brains of patients with Alzheimer disease. In addition, two of the peptides are antimicrobial peptides, having been shown to have bacteriocidal and antifungal activities. Mutations in this gene have been implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy). Multiple transcript variants encoding several different isoforms have been found for this gene. [provided by RefSeq, Aug 2014] Product datasheet: Overview Product Description APP encodes a cell surface receptor and transmembrane precursor protein that is cleaved by secretases to form a number of peptides. Some of these peptides are secreted and can bind to the acetyltransferase complex APBB1/TIP60 to promote transcriptional activation, while others form the protein basis of the amyloid plaques found in the brains of patients with Alzheimer disease. Mutations in this gene have been implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy). Multiple transcript variants encoding several different isoforms have been found for this gene. Tested Applications WB Image Western blot analysis of extracts from Hela cells, treated with Noc or calf intestinal phosphatase (CIP), using APP (Phospho-Thr668) Antibody #11190. Western blot analysis of extracts from mouse brain tissue using APP (Phospho-668) Antibody #11190 (Lane 2) and the same antibody preincubated with blocking peptide (Lane1). Species Reactivities Human Mouse Rat Immunogen Peptide sequence around phosphorylation site of threonine 668 (A-V-T(p)-P-E) derived from Human APP. Properties Storage Instructions Store at -20C Clonality Polyclonal Antibody References: Key roles of Tyr 10 in Cu bound A complexes and its relevance to Alzheimer's disease. Lu N, et al. Arch Biochem Biophys, 2015 Oct 15. PMID 26247837 Design and Characterization of Chemically Stabilized A42 Oligomers. Yamin G, et al. Biochemistry, 2015 Sep 1. PMID 26241378 Mechanism of Nucleated Conformational Conversion of A42. Fu Z, et al. Biochemistry, 2015 Jul 14. PMID 26069943 [The role of zinc ions and structural polymorphism of -amyloid in the Alzheimer's disease initiation]. Kulikova AA, et al. Mol Biol (Mosk), 2015 Mar-Apr. PMID 26065253 Three dimensions of the amyloid hypothesis: time, space and 'wingmen'. Musiek ES, et al. Nat Neurosci, 2015 Jun. PMID 26007213
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