Anti-Beta Amyloid APP Antibody

Beta amyloid, often abbreviated as A-beta, is a protein that builds up in the brains of persons with Alzheimer's disease, collecting in clumps called plaques or senile plaques. While some researchers question whether beta amyloid is the cause of the dementia, most agree that it is involved in the disruption of thinking that is a hallmark of the disease. In some cases of familial Alzheimer's disease, mutations in genes for the proteins called the presenilins lead to increased production of amyloid. Researchers have been looking at how presenilin-1 in particular contributes to the excess buildup of beta amyloid. Presenilin-1 apparently acts to increase the activity of gamma-secretase, an enzyme that changes a normal protein (amyloid precursor protein or APP) into beta amyloid itself. Furthermore, presenilin-1 might be gamma-secretase. Anti-Beta Amyloid Antibody is useful for researchers interested in TLR signaling and Alzheimer's research.

This antibody was affinity purified from whole rabbit serum prepared by repeated immunizations with a synthetic peptide corresponding to an extracellular region of human beta amyloid conjugated to KLH using maleimide.

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

This affinity purified antibody is directed against extracellular region of beta amyloid and is useful in determining its presence in various assays. Polyclonal anti-beta amyloid detects human and mouse beta amyloid. Blast analysis of the sequence of the immunogen shows 100% identity with Human, Guinea Pig, Pig, Cyno Monkey, Dog, Polar Bear, Rabbit, Chimp, Squirrel monkey, and Sheep. Cross-reactivity with beta amyloid from other species is likely but has not been determined.

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.

Store vial at -20°C prior to opening. Aliquot contents and freeze at -20°C or below for extended storage. Avoid cycles of freezing and thawing. Centrifuge product if not completely clear after standing at room temperature. This product is stable for several weeks at 4°C as an undiluted liquid. Dilute only prior to immediate use. Expiration date is one (1) year from date of opening.

Affinity purified anti-beta amyloid has been tested by ELISA, IHC, WB, and IF. A 45.8kDa band is detected in western blot using whole tissue extracts and lysates from mouse and human. In general, we recommend the use of 4% PFA or 10% formalin for fixation of tissues with IHC-paraffin or IHC-frozen application of this antibody.

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.