抗淀粉样β1-42抗体_详细资料

产品信息

抗淀粉样β1-42抗体OverviewProduct nameAnti-beta Amyloid 1-42 antibodySee all beta Amyloid 1-42 products ( 3 ) ... DescriptionRabbit polyclonal to beta Amyloid 1-42SpecificityThis 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

抗淀粉样β1-42抗体
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 100 µl at 0.5 mg/ml

Concentration information loading...

PurityProtein G purified

Clonality Polyclonal

IsotypeIgG

Research Areas

Neuroscience

Neurology process

Neurodegenerative disease

Alzheimer＇s disease

Amyloid

Applications
Our Abpromise guarantee covers the use of ab10148 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Notes

IHC-P IHC-P: Use at an assay dependent dilution. Retrieve antigens with 70% Formic acid for 10-30 minutes at room temperature before commencing with IHC staining protocol.

IHC-Fr IHC-Fr: Use at an assay dependent dilution. PubMed: 18673368

ICC ICC: Use at an assay dependent concentration. PubMed: 22003387

WB WB: Use at an assay dependent dilution. PubMed: 19151372

Application notesIs unsuitable for or ELISA.
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

Application	Notes
IHC-P	IHC-P: Use at an assay dependent dilution. Retrieve antigens with 70% Formic acid for 10-30 minutes at room temperature before commencing with IHC staining protocol.
IHC-Fr	IHC-Fr: Use at an assay dependent dilution. PubMed: 18673368
ICC	ICC: Use at an assay dependent concentration. PubMed: 22003387
WB	WB: Use at an assay dependent dilution. PubMed: 19151372

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