Anti-beta Amyloid 1-42 antibody (ab10148)

Overview

• Product nameAnti-beta Amyloid 1-42 antibodySee all beta Amyloid 1-42 primary antibodies ...
• Description
  Rabbit polyclonal to beta Amyloid 1-42
• SpecificityThis antibody is reactive with A Beta 42 and does not cross-react with A beta Amyloid 1-40, full-length APP, sAPP beta or sAPP alpha. We have evaluated this antibody by IHC and have not specifically evaluated reactivity with oligomeric forms of beta amyloid.
• Tested applicationsIHC-P, IHC-Fr, ICC, WB more details
• Species reactivity
  Reacts with: Mouse, Rat, Dog, Human
  
• Immunogen

  Synthetic peptide conjugated to KLH, corresponding to amino acids 33-42 of Human beta Amyloid 1-42.

• General notesDo not store antibody diluted below 0.5 mg/ml

Properties

• FormLiquid
• Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
• Storage bufferPreservative: None
  Constituents: PBS
• Concentration information loading...
• PurityProtein G purified
• Clonality Polyclonal
• IsotypeIgG
• Research Areas
  • Neuroscience
  • Neurology process
  • Neurodegenerative disease
  • Alzheimer's disease
  • Amyloid

Applications

Target

• FunctionFunctions 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.
  Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), 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 overexpressed HADH2 leads to oxidative stress and neurotoxicity.
  Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain.
  The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis.
  N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).
• Tissue specificityExpressed 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.
• Involvement in diseaseDefects in APP are the cause of Alzheimer disease type 1 (AD1) [MIM:104300]. AD1 is a familial early-onset form of Alzheimer disease. It can be associated with cerebral amyloid angiopathy. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death.
  Defects in APP are the cause of cerebral amyloid angiopathy APP-related (CAA-APP) [MIM:605714]. A hereditary localized amyloidosis due to amyloid-beta A4 peptide(s) deposition in the cerebral vessels. The principal clinical characteristics are recurrent cerebral and cerebellar hemorrhages, recurrent strokes, cerebral ischemia, cerebral infarction, and progressive mental deterioration. Patients develop cerebral hemorrhage because of the severe cerebral amyloid angiopathy. Parenchymal amyloid deposits are rare and largely in the form of pre-amyloid lesions or diffuse plaque-like structures. They are Congo red negative and lack the dense amyloid cores commonly present in Alzheimer disease. Some affected individuals manifest progressive aphasic dementia, leukoencephalopathy, and occipital calcifications.
• Sequence similaritiesBelongs to the APP family.
  Contains 1 BPTI/Kunitz inhibitor domain.
• DomainThe basolateral sorting signal (BaSS) is required for sorting of membrane proteins to the basolateral surface of epithelial cells.
  The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain. However, additional amino acids either N- or C-terminal to the NPXY motif are often required for complete interaction. The PID domain-containing proteins which bind APP require the YENPTY motif for full interaction. These interactions are independent of phosphorylation on the terminal tyrosine residue. The NPXY site is also involved in clathrin-mediated endocytosis.
• Post-translational
  modificationsProteolytically 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 40 (Abeta40) and amyloid-beta 42 (Abeta42), major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59).
  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 beta-amyloid peptides.
  N- and O-glycosylated. O-linkage of chondroitin sulfate to the L-APP isoforms produces the APP proteoglycan core proteins, the appicans. The chondroitin sulfate chain of appicans contains 4-O-sulfated galactose in the linkage region and chondroitin sulfate E in the repeated disaccharide region.
  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 beta-amyloid-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).
  Beta-amyloid peptides are degraded by IDE.
• Cellular localizationMembrane. 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.

Target information above from: UniProt accession P05067 The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010) .

Information by UniProt
• Database links
  • Entrez Gene: 351 Human
  • Entrez Gene: 11820 Mouse
  • Entrez Gene: 11820 Mouse
  • Entrez Gene: 54226 Rat
  • Omim: 104760 Human
  • SwissProt: P05067 Human
  • SwissProt: P12023 Mouse
  • SwissProt: P08592 Rat

  • Unigene: 434980 Human
  • Unigene: 277585 Mouse
  • Unigene: 2104 Rat

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• Alternative names
  A4 antibodyA4_HUMAN antibodyAAA antibody

  ABETA antibodyABPP antibodyAD1 antibodyAICD-50 antibodyAICD-57 antibodyAICD-59 antibodyAID(50) antibodyAID(57) antibodyAID(59) antibodyAlzheimer disease 1 antibodyAlzheimer disease amyloid protein antibodyAmyloid beta (A4) precursor protein antibodyAmyloid beta A4 protein antibodyAmyloid beta peptide antibodyAmyloid intracellular domain 50 antibodyAmyloid intracellular domain 57 antibodyAmyloid intracellular domain 59 antibodyAmyloid of aging and Alzheimer disease antibodyAPP antibodyAPPI antibodyb Amyloid peptide antibodybeta Amyloid antibodyBeta amyloid protein 42 antibodyBeta APP42 antibodyBeta-APP40 antibodyBeta-APP42 antibodyC31 antibodyCerebral vascular amyloid peptide antibodyCTFgamma antibodyCVAP antibodyGamma-CTF(50) antibodyGamma-CTF(57) antibodyGamma-CTF(59) antibodyPeptidase nexin II antibodyPN II antibodyPN-II antibodyPN2 antibodyPreA4 antibodyProtease nexin II antibodyProtease nexin-II antibodyS-APP-alpha antibodyS-APP-beta antibody

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Anti-beta Amyloid 1-42 antibody images

• 

  Immunohistochemistry (Formalin-fixed paraffin-embedded sections) - beta Amyloid 1-42 antibody (ab10148)

  ab10148 at a 1/50 dilution staining mouse AD brain tissue sections by Immunohistochemistry (Formalin-fixed paraffin-embedded sections). Following heat mediated antigen retrieval, the antibody was incubated with the tissue for 24 hours. Bound antibody was detected using a biotinylated Goat anti-Rabbit antibody.

  This image is courtesy of an Abreview submitted on 15 March 2006.

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• 

  Immunohistochemistry (Frozen sections) - beta Amyloid 1-42 antibody (ab10148)This image is courtesy of an anonymous Abreview

  ab10148 staining mouse skeletal muscle tissue sections by IHC-Fr.  Sections were acetone fixed and blocked in 5% BSA for 30 minutes at RT prior to incubating with ab10148, diluted 1/100, for 12 hours at 4°C. A FITC conjugated goat anti-rabbit antibody, diluted 1/200, was used as the secondary.

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