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Anti-Amyloid β 1-16 Antibody (57004)

$471.00

Host Quantity Applications Species Reactivity Data Sheet  
Mouse 100ug WB,IHC,IF,IP,ELISA Human, Mouse
SKU: 57004 Categories: , , ,
Overview
Product Name Anti-Amyloid β 1-16 Antibody (57004)
Description Anti-Amyloid β 1-16 Mouse Monoclonal Antibody
Target Amyloid β 1-16
Species Reactivity Human, Mouse
Applications WB,IHC,IF,IP,ELISA
Host Mouse
Clonality Monoclonal
Clone ID Ab5
Isotype IgG2b
Immunogen Aggregated Ab1-42, fibrillar Ab.
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 recognizes an epitope within Ab1-16 as well as other Ab peptides: Ab37, Ab38, Ab39, Ab40, and Ab42. NOTE: When administered to young Tg2576 mice with minimal Ab deposition and to older mice with higher Ab loads, this antibody reduced Ab accumulation in the brain.
Target Name Amyloid-β precursor protein
Target ID Amyloid β 1-16
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). There is now compelling evidence that metal binding to Abeta is involved in AD pathogenesis. The amino acid region 1-16 is widely considered as the metal binding domain of Abeta. Unlike copper(II) that prefers the N-terminal amino group as the main binding site, zinc(II) is preferentially placed in the 8-16 amino acidic region of Abeta (1-16).
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 in all applications.

Sandwich ELISA as capture or 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.