APP blocking peptide

APP Antibody (C-term) Blocking Peptide

• Gene Names: APP; AAA; AD1; PN2; ABPP; APPI; CVAP; ABETA; PN-II; CTFgamma
• Synonyms: APP; APP Antibody (C-term) Blocking Peptide; Amyloid beta A4 protein; ABPP; APPI; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; PreA4; Protease nexin-II; PN-II; N-APP; Soluble APP-alpha; S-APP-alpha; Soluble APP-beta; S-APP-beta; C99; Beta-amyloid protein 42; Beta-APP42; Beta-amyloid protein 40; Beta-APP40; C83; 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; A4; AD1; APP blocking peptide

• Specificity: The synthetic peptide sequence used to generate the antibody was selected from the C-term region of human APP. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
• Form/Format: The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.
• Sequence Length: 770

• Cellular Location: Membrane; Single-pass type I membrane protein. Membrane, clathrin-coated pit. Note: Cell surface protein that rapidly becomes internalized via clathrin-coated pits. During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. Gamma-CTF(59) peptide is located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65). Beta-APP42 associates with FRPL1 at the cell surface and the complex is then rapidly internalized. APP sorts to the basolateral surface in epithelial cells. During neuronal differentiation, the Thr-743 phosphorylated form is located mainly in growth cones, moderately in neurites and sparingly in the cell body. Casein kinase phosphorylation can occur either at the cell surface or within a post-Golgi compartment. Associates with GPC1 in perinuclear compartments. Colocalizes with SORL1 in a vesicular pattern in cytoplasm and perinuclear regions
• Tissue Location: 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
• Preparation and Storage: Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C.

Related Product Information for APP blocking peptide

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 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. N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).

NCBI and Uniprot Product Information

• NCBI GI #: 112927
• NCBI GeneID: 351
• UniProt Accession #: P05067; P09000; P78438; Q13764; Q13778; Q13793; Q16011; B2R5V1; B4DII8; D3DSD1; D3DSD2; D3DSD3
• Molecular Weight: 84,521 Da
• NCBI Official Full Name: Amyloid beta A4 protein
• NCBI Official Synonym Full Names: amyloid beta precursor protein
• NCBI Official Symbol: APP
• NCBI Official Synonym Symbols: AAA; AD1; PN2; ABPP; APPI; CVAP; ABETA; PN-II; CTFgamma
• NCBI Protein Information: amyloid beta A4 protein
• UniProt Protein Name: Amyloid beta A4 protein
• Protein Family: Amyloid beta A4 protein
• UniProt Gene Name: APP
• UniProt Synonym Gene Names: A4; AD1; APP; CVAP; PN-II; S-APP-alpha; S-APP-beta; AICD-59; AID(59); AICD-57; AID(57); AICD-50; AID(50)
• UniProt Entry Name: A4_HUMAN

NCBI Description

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]

Uniprot Description

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

Chromosomal Location of Human Ortholog: 21q21.3

Cellular Component: axon; cell surface; cytoplasm; cytosol; dendritic shaft; dendritic spine; endosome; extracellular region; extracellular space; Golgi apparatus; integral to membrane; integral to plasma membrane; intracellular membrane-bound organelle; lipid raft; nuclear envelope lumen; perinuclear region of cytoplasm; plasma membrane; receptor complex; synapse; trans-Golgi network membrane

Molecular Function: DNA binding; enzyme binding; identical protein binding; protein binding; PTB domain binding; receptor binding; serine-type endopeptidase inhibitor activity

Biological Process: adult locomotory behavior; axon cargo transport; axon midline choice point recognition; axonogenesis; cellular copper ion homeostasis; cellular process; cellular protein metabolic process; collateral sprouting in the absence of injury; dendrite development; endocytosis; extracellular matrix organization and biogenesis; innate immune response; ionotropic glutamate receptor signaling pathway; locomotory behavior; mating behavior; mRNA polyadenylation; neurite development; neuron apoptosis; neuron remodeling; platelet degranulation; positive regulation of mitotic cell cycle; protein amino acid phosphorylation; regulation of epidermal growth factor receptor activity; regulation of multicellular organism growth; regulation of synapse structure and activity; regulation of translation; visual learning

Disease: Alzheimer Disease