Awaiting product image

Anti-Amyloid β 1-42 Antibody (57001)

Host Quantity Applications Species Reactivity Data Sheet  
Mouse 100ug WB,IHC,IF,IP,ELISA Human, Mouse
Buy Now on Leinco.com
SKU: 57001 Categories: , , ,
Overview
Product Name Anti-Amyloid β 1-42 Antibody (57001)
Description Anti-Amyloid β 1-42 Mouse Monoclonal Antibody
Target Amyloid β 1-42
Species Reactivity Human, Mouse
Applications WB,IHC,IF,IP,ELISA
Host Mouse
Clonality Monoclonal
Clone ID Ab42.2
Isotype IgG1
Immunogen Synthetic peptide correspond- ing to Ab35-42.
Properties
Form Liquid
Concentration Lot Specific
Formulation PBS, pH 7.4.
Buffer Formulation Phosphate Buffered Saline
Buffer pH pH 7.4
Format Purified
Purification Purified by Protein G affinity chromatography
Specificity Information
Specificity This antibody specifically recognizes an epitope within Abx-42. NOTE: When administered to young Tg2576 mice with minimal Ab deposition, this antibody reduced Ab accumulation in the brain.
Target Name Amyloid-β precursor protein
Target ID Amyloid β 1-42
Uniprot ID P05067
Alternative Names APP, ABPP, APPI, Alzheimer disease amyloid A4 protein homolog, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-β
Gene Name APP
Sequence Location Cell membrane, Membrane, Perikaryon, Cell projection, growth cone, Membrane, clathrin-coated pit, Early endosome, Cytoplasmic vesicle
Biological Function Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis (PubMed:25122912). 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 (By similarity). By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapes in axons (PubMed:17062754, PubMed:23011729). 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. {UniProtKB:P12023, PubMed:17062754, PubMed:23011729, PubMed:25122912}.; Amyloid-beta 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. Amyloid-beta protein 42 is a more effective reductant than amyloid-beta protein 40. Amyloid-beta peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. APP42-beta 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. Also binds GPC1 in lipid rafts.; Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain. {ECO:0000250}.; 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).
Research Areas Neuroscience
Background Accumulation and aggregation of amyloid beta (Abeta) in the brain is indicated as the trigger of a pathological cascade that causes Alzheimer disease (AD). The highly amyloidogenic 42-amino acid form of Abeta (Abeta42) and aminoterminally truncated forms of Abeta (Abetax-42) are the predominant species of Abeta typically found in diffuse and senile plaques within the AD brain. The relative levels of Abeta42 appear to be the key regulators of Abeta aggregation into amyloid; thus Abeta42 has been implicated as the initiating molecule in the pathogenesis of AD.
Application Images
Additional Information
Handling
Storage This antibody is stable for at least one (1) year at -20°C.
Dilution Instructions Dilute in PBS or medium that is identical to that used in the assay system.
Application Instructions Immunoblotting,

Immunohistochemistry: Immunofluorescence, Immunoprecipitation Test at 1-10ug/ml.Sandwich ELISA (as capture antibody with #57004 as HRP-conjugated detection antibody).

These are recommended concentrations

End user should determine optimal concentrations for their applications.Sandwich ELISA protocol on next page. See specific product references below for more information.
References & Data Sheet
References Levites Y et al. 2006. Anti-Ab42 and Anti-Ab40 specific monoclonal antibodies attenuate amyloid deposition in an Alzheimer's disease mouse model. J Clin Invest 116: 193-201.
Levites Y et al. 2006. Intracranial Adeno-Associated Virus-Mediated Delivery of Anti-Pan Amyloid b, Amyloidb40, and Amyloid b42 Single-Chain Variable Fragments Attenuates Plaque Pathology in Amyloid Precursor Protein Mice. J Neurosci 26: 11923-11928.
Levites Y et al. 2006. Insights into the mechanisms of action of anti-Ab antibodies in Alzheimer's disease mouse models. FASEB J 20: 2576-8.
Ilieviski, et al. 2018. PLoS One . 2018 Oct 3
13(10):e0204941.