Our Anti-Amyloid Precursor Protein rabbit polyclonal primary antibody from PhosphoSolutions is produced in-house. It detects mouse and rat Amyloid Precursor Protein and is antigen affinity purified from pooled serum. It is great for use in WB.
Western blot of rat hippocampal lysate showing specific immunolabeling of the ~115 kDa APP protein.
A large body of evidence has implicated the amyloid precursor protein (APP) in the pathogenesis of Alzheimer's disease (AD) (Kamenetz et al., 2003). The phosphorylation of APP at Thr668 is thought to play a critical role in generation of the soluble APP (beta) and beta-amyloid peptide (abeta) which are the major components of senile plaques in patient brains inflicted with AD (Liu et al., 2003; Ando et al., 2001).
Antigen Affinity Purified from Pooled Serum
Polyclonal
IgG
ELISA, WB
Rabbit
APP
115 kDa
Synthetic peptide corresponding to amino acid residues from the C-terminal region of rat APP, conjugated to keyhole limpet hemocyanin (KLH).
Rat
Mouse, Rat
Canine, Chicken, Human, Non-Human Primate
AB_2492039
Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.
Liquid
Prepared from rabbit serum by affinity purification on a column made with the C-terminal peptide used as antigen.
10 mM HEPES (pH 7.5), 150 mM NaCl, 100 µg per ml BSA and 50% glycerol.
WB: 1:1000
WB Brain: 1:1000
Unconjugated
Specific for endogenous levels of the ~115 kDa APP protein. Immunolabeling of the APP protein band is completely blocked by preadsorption of the antibody with the peptide used as antigen.
Western blots performed on each lot.
For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.
After date of receipt, stable for at least 1 year at -20°C.
P08592
UniProt Summary: 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 (PubMed:25122912). 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 (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapses in axons (PubMed:17062754, PubMed:23011729). 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. {ECO:0000250, ECO:0000250|UniProtKB:P12023, ECO:0000269|PubMed:17062754, ECO:0000269|PubMed:23011729, ECO:0000269|PubMed:25122912}.; 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 peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. 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.; [Amyloid-beta protein 42]: More effective reductant than amyloid-beta protein 40. May activate mononuclear phagocytes in the brain and elicit inflammatory responses.; Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain. {ECO:0000250}.; The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis.
Ando K, Iijima KI, Elliott JI, Kirino Y, Suzuki T (2001) Phosphorylation-dependent regulation of the interaction of amyloid precursor protein with Fe65 affects the production of beta-amyloid. J Biol Chem 276:40353-40361. PMID: 11517218
Kamenetz, F., Tomita, T., Hsieh, H., Seabrook, G., Borchelt, D., Iwatsubo, T., Sisodia, S. and Malinow, R., 2003. APP processing and synaptic function. Neuron, 37(6), pp.925-937. PMID: 12670422
Liu F, Su Y, Li B, Zhou Y, Ryder J, Gonzalez-DeWhitt P, May PC, Ni B (2003) Regulation of amyloid precursor protein (APP) phosphorylation and processing by p35/cdk5 and p25/cdk5. FEBS Lett 547:193-196. PMID: 12860412
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