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Rabbit Anti-APP Polyclonal Antibody#abs135532

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Description

Catalog-specification	Delivery time	USD price
abs135532-50ug	1-2 Weeks	201.0
abs135532-100ug	1-2 Weeks	301.0

Overview
catalog	abs135532
Description	The transmembrane glycoprotein known as amyloid β (Aβ) precursor protein (APP) has a molecular weight ranging from 100 to 140 kDa. It is characterized by its various isoforms. One notable feature of the APP's amino acid sequence is the presence of the amyloid domain (Aβ). This particular domain can be liberated through a two-step proteolytic cleavage process. The accumulation and deposition of the released Aβ fragments in the extracellular space are pivotal components of amyloid plaques, a hallmark of Alzheimer's disease. The proteolytic processing and secretion of APP can be influenced by its phosphorylation at multiple sites. Notably, phosphorylation at Thr668 (specifically in the APP695 isoform) is cell cycle-dependent and reaches its peak during the G2/M-phase. Adult rat brain has been found to harbor APP phosphorylated at Thr668, which also correlates with neuronal differentiation in cultured cells.
Other names	The amyloid beta protein, also known as A4 protein or APP, has been implicated in Alzheimer's disease. It is a precursor protein that is processed into beta-amyloid peptides, which can accumulate and form plaques in the brain. The intracellular domain of the protein, known as AICD, has also been studied for its potential role in neurodegeneration. Other fragments of the protein, such as CTFgamma and CVAP, have also been associated with Alzheimer's disease. Peptidase nexin-II (PN-II) is an inhibitor of the enzyme that cleaves APP, and may also play a role in the pathology of Alzheimer's. Understanding the molecular mechanisms involved in APP processing and regulation may lead to the development of new therapies for the treatment of Alzheimer's disease.
Source	Rabbit
Specificity	The endogenous levels of total APP can be detected by using the APP Antibody. A content can be generated based on the original information by rearranging the text.
Species Reactivity	Human;Mouse;Rat
Antigen	APP
Application	The recommended dilutions for using this antibody are as follows: 1:500-1:2000 for Western blotting, 1:50-1:200 for immunohistochemistry, 1:10-1:100 for immunofluorescence, and 1:20000-1:40000 for ELISA assays using peptide substrates. These dilutions ensure optimal results and minimal background signal. Please note that higher dilutions may be necessary for some applications, depending on the sample type and target protein expression levels. It is always recommended to perform a titration experiment to determine the optimal working dilution for your specific experiment.
Immunogen	N term -peptideof human APP.
MW	87kDa,100kDa
Properties
Concentration	1mg/ml
purification	The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin .
Clonality	Polyclonal Antibody
Stability & Storage	Store at -20 °C for one year. Avoid repeated freeze/thaw cycles
Storage buffer	Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.Store at -20 °C.Stable for 12 months from date of receipt.
Target
Background	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.
Tissue specificity	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.
Posttranslational modification	Proteolytically processed under normal cellular conditions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid-beta proteins, amyloid-beta protein 40 and amyloid-beta protein 42, major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). Many other minor amyloid-beta peptides, amyloid-beta 1-X peptides, are found in cerebral spinal fluid (CSF) including the amyloid-beta X-15 peptides, produced from the cleavage by alpha-secretase and all terminating at Gln-686.Proteolytically cleaved by caspases during neuronal apoptosis. Cleavage at Asp-739 by either caspase-6, -8 or -9 results in the production of the neurotoxic C31 peptide and the increased production of amyloid-beta peptides.N- and O-glycosylated. O-glycosylation on Ser and Thr residues with core 1 or possibly core 8 glycans. Partial tyrosine glycosylation (Tyr-681) is found on some minor, short amyloid-beta peptides (amyloid-beta 1-15, 1-16, 1-17, 1-18, 1-19 and 1-20) but not found on amyloid-beta protein 38, amyloid-beta protein 40 nor on amyloid-beta protein 42. Modification on a tyrosine is unusual and is more prevelant in AD patients. Glycans had Neu5AcHex(Neu5Ac)HexNAc-O-Tyr, Neu5AcNeu5AcHex(Neu5Ac)HexNAc-O-Tyr and O-AcNeu5AcNeu5AcHex(Neu5Ac)HexNAc-O-Tyr structures, where O-Ac is O-acetylation of Neu5Ac. Neu5AcNeu5Ac is most likely Neu5Ac 2,8Neu5Ac linked. O-glycosylations in the vicinity of the cleavage sites may influence the proteolytic processing. Appicans are L-APP isoforms with O-linked chondroitin sulfate.Phosphorylation in the C-terminal on tyrosine, threonine and serine residues is neuron-specific. Phosphorylation can affect APP processing, neuronal differentiation and interaction with other proteins. Phosphorylated on Thr-743 in neuronal cells by Cdc5 kinase and Mapk10, in dividing cells by Cdc2 kinase in a cell-cycle dependent manner with maximal levels at the G2/M phase and, in vitro, by GSK-3-beta. The Thr-743 phosphorylated form causes a conformational change which reduces binding of Fe65 family members. Phosphorylation on Tyr-757 is required for SHC binding. Phosphorylated in the extracellular domain by casein kinases on both soluble and membrane-bound APP. This phosphorylation is inhibited by heparin.Extracellular binding and reduction of copper, results in a corresponding oxidation of Cys-144 and Cys-158, and the formation of a disulfide bond. In vitro, the APP-Cu+ complex in the presence of hydrogen peroxide results in an increased production of amyloid-beta-containing peptides.Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP).Amyloid-beta peptides are degraded by IDE.
Celluar localization	Cytoskeleton;Cytosol;Endoplasmic reticulum;Endosome;Extracellular region or secreted;Golgi apparatus;Nucleus;Plasma Membrane;
UniPort	P05067