Anti-beta Amyloid/APP Antibody Picoband® Fluoro488 Conjugated

Beta Amyloid, also called Abeta or Abeta, denotes peptides of 36–43 amino acidsthat are crucially involved in Alzheimer's disease as the main component of the amyloid plaques found in the brains of Alzheimer patients. It is mapped to 19q13.12. Several potential activities have been discovered for beta Amyloid, including activation of kinase enzymes, functioning as atranscription factor, and anti-microbial activity (potentially associated with beta Amyloid's pro-inflammatoryactivity) . Moreover, monomeric beta Amyloid is indicated to protect neurons by quenching metal-inducible oxygen radical generation and thereby inhibiting neurotoxicity.

Amyloid beta A4 protein; ABPP; APPI; APP; 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; APP; A4, AD1

A synthetic peptide corresponding to a sequence at the C-terminus of human APP, different from the related mouse and rat sequences by three amino acids.

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. .

Adapters, Apoptosis, Associated Proteins, Cell Biology, Cytoplasmic, Developmental Biology, Intracellular, Nervous System Development, Neural Signal Transduction, Neurogenesis, Neurology Process, Neuroscience, Organelle Proteins, Organogenesis, Protein Trafficking, Signal Transduction

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 ly 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. .

1. Zou K, Gong JS, Yanagisawa K, Michikawa M (June 2002) . A novel function of monomeric amyloid beta-protein serving as an antioxidant molecule against metal-induced oxidative damage.J. Neurosci. 22 (12) : 4833–41. 2. Tabaton M, Zhu X, Perry G, Smith MA, Giliberto L (January 2010) . Signaling Effect of Amyloid-β42 on the Processing of AβPP. Exp. Neurol. 221 (1) : 18–25. 3. Baruch-Suchodolsky R, Fischer B (May 2009) . Abeta40, either soluble or aggregated, is a remarkably potent antioxidant in cell-free oxidative systems. Biochemistry 48 (20) : 4354–70. 4. Igbavboa U, Sun GY, Weisman GA, He Y, Wood WG (August 2009) . Amyloid β-Protein Stimulates Trafficking of Cholesterol and Caveolin-1 from the Plasma Membrane to the Golgi Complex in Mouse Primary Astrocytes. Neuroscience 162 (2) : 328–38.

Membrane; Single-pass type I membrane protein. Membrane, clathrin-coated pit. 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.