ABPP; APPI; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; PreA4; Protease nexin-II; A4; AD1; APP

For Research Use Only. Not for use in diagnostic procedures.

Polyclonal

IgG

Rabbit

Caprylic Acid Ammonium Sulfate Precipitation Purified

Shipped at 4 degree C. Upon delivery aliquot and store at -20 degree C or -80 degree C. Avoid repeated freeze.

Manufactured in an ISO 13485:2003 and EN ISO 13485:2012 Certified Laboratory.

Small volumes of anti-APP antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. 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. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu2+-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 Cu2+ ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1. Ref.38 Ref.65 Ref.67 Ref.90 Ref.91 Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu2+ and Fe3+ to Cu+ and Fe2+, respectively. Beta-amyloid 42 is a more effective reductant than beta-amyloid 40. Beta-amyloid peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with Also bind GPC1 in lipid rafts.

ELISA (EIA)

84,521 Da[Similar Products]

amyloid beta precursor protein

amyloid beta A4 protein

Amyloid beta A4 protein

A4; AD1; APP; CVAP; PN-II; S-APP-alpha; S-APP-beta; AICD-59; AID(59); AICD-57; AID(57); AICD-50; AID(50)??[Similar Products]

A4_HUMAN

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]

APP: a cell surface receptor that influences neurite growth, neuronal adhesion and axonogenesis. Cleaved by secretases to form a number of peptides, some of which bind to the acetyltransferase complex Fe65/TIP60 to promote transcriptional activation. The Abeta peptide is released from the cell, its extracellular deposition and accumulation form the main components of amyloid plaques in Alzheimer's disease. Mutations in this gene have been implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis. Can promote transcription activation through binding to Fe65-Tip60 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. 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. Induces a RAGE-dependent pathway that activates 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. Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, JIP1, SHC1 and, NUMB and DAB1. Binding to DAB1 inhibits its serine phosphorylation. Associates with microtubules in the presence of ATP and in a kinesin-dependent manner. Amyloid beta-42 binds nAChRA7 in hippocampal neurons. Beta-amyloid associates with HADH2. Soluble APP binds, via its N-terminal head, to FBLN1. Expressed in all fetal tissues examined with highest levels in brain, kidney, heart and spleen. Weak expression in liver. In ***** 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. 10 isoforms of the human protein are produced by alternative splicing. 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. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Belongs to the APP family.

Protein type: Apoptosis; Receptor, misc.; Membrane protein, integral; Cell surface; Transcription factor

Chromosomal Location of Human Ortholog: 21q21.3

Cellular Component: apical part of cell; axon; cell surface; ciliary rootlet; coated pit; cytoplasm; cytosol; dendritic shaft; dendritic spine; endosome; ER to Golgi transport vesicle; extracellular region; extracellular space; Golgi apparatus; integral to membrane; integral to plasma membrane; intercellular junction; intracellular membrane-bound organelle; lipid raft; neuromuscular junction; nuclear envelope lumen; perinuclear region of cytoplasm; plasma membrane; receptor complex; rough endoplasmic reticulum; smooth endoplasmic reticulum; spindle midzone; synapse; terminal button; trans-Golgi network membrane

Molecular Function: acetylcholine receptor binding; DNA binding; enzyme binding; heparin binding; identical protein binding; protease activator activity; protein binding; PTB domain binding; receptor binding; serine-type endopeptidase inhibitor activity; transition metal ion binding

Biological Process: ***** locomotory behavior; antibacterial humoral response; antifungal humoral response; axon cargo transport; axon midline choice point recognition; axonogenesis; blood coagulation; cell adhesion; cellular copper ion homeostasis; cellular protein metabolic process; cholesterol metabolic process; collateral sprouting in the absence of injury; defense response to Gram-negative bacterium; defense response to Gram-positive bacterium; dendrite development; endocytosis; extracellular matrix organization and biogenesis; forebrain development; innate immune response; ionotropic glutamate receptor signaling pathway; locomotory behavior; mating behavior; mRNA polyadenylation; negative regulation of neuron differentiation; neurite development; neuromuscular process controlling balance; neuron apoptosis; neuron remodeling; Notch signaling pathway; platelet activation; platelet degranulation; positive regulation of mitotic cell cycle; positive regulation of transcription from RNA polymerase II promoter; post-Golgi vesicle-mediated transport; protein amino acid phosphorylation; regulation of epidermal growth factor receptor activity; regulation of multicellular organism growth; regulation of protein binding; regulation of synapse structure and activity; regulation of translation; response to lead ion; response to oxidative stress; response to yeast; smooth endoplasmic reticulum calcium ion homeostasis; suckling behavior; synaptic growth at neuromuscular junction; visual learning

Disease: Alzheimer Disease

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