Rabbit Polyclonal Amyloid-beta antibody (STJ98585)

$99.00$319.00

Reactivity: Human, Mouse, Rat
Applications: WB, IHC, IF, ELISA
Conjugation: Unconjugated
Supplier: St John’s Laboratory Ltd.

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Rabbit Polyclonal Amyloid-beta antibody (STJ98585)

Supplier: St John’s Laboratory Ltd.

Recommended applications: WB, ELISA

Recommended dilution: WB 1:500-2000; ELISA 1:10000-20000

Recommended protocols: check protocols

Image descriptions:

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Alternative names:

Check alternative names for the antibody

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APP antibody, A4 antibody, AD1 antibody,|AAA antibody|AAAS antibody|AAASb antibody|Achalasia adrenocortical insufficiency alacrimia (Allgrove triple A) antibody|Achalasia adrenocortical insufficiency alacrimia antibody|ADRACALA antibody|ADRACALIN antibody|Aladin antibody|Allgrove triple A antibody|DKFZp586G1624 antibody|GL003 antibody|Anti-Amyloid Fibril antibody [mOC87] – Conformation-Specific (ab201062)
SCBT cat No: sc-53822|sc-28365|sc-374527|sc-5399|sc-58508|sc-9129|sc-65642|sc-32277|sc-53780|sc-9182|sc-6389|sc-6390|

Name

Amyloid-beta Polyclonal Antibody

Catalogue No.

STJ98585

Reactivity

Human, Mouse, Rat

Specificity

Amyloid-beta Polyclonal Antibody detects endogenous levels of Amyloid-beta

Immunogen

Synthesized peptide derived from Amyloid-beta at AA range 221-270

Host

Rabbit

Applications

WB, ELISA

Recommended dilution

WB 1:500-2000; ELISA 1:10000-20000

Clonality

Polyclonal

Conjugation

Unconjugated

Formulation

Amyloid-beta Antibody was tube-contained. Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.

Concentration

1 mg/ml

Purification

Amyloid-beta Antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.

Storage

-20 Celsius degree. Avoid repeated freeze/thaw cycles.

Alternative antibody names

Amyloid beta A4 protein antibody, ABPP antibody, APPI antibody, APP antibody, Alzheimer disease amyloid protein antibody, Amyloid precursor protein antibody, Beta-amyloid precursor protein antibody, Cerebral vascular amyloid peptide antibody, CVAP antibody, PreA4 antibody, Protease nexin-II antibody, PN-II antibody

Database links

Human UniProt/Swiss-Prot:P05067;Mouse UniPort/Swiss-Prot: P12023;Rat UniProt/Swiss-Port: P08592;Human Entrez Gene: 351;Mouse Entrez Gene: 11820;Rat Entrez Gene: Rn.2104

Protein names

Amyloid beta A4 protein , ABPP , APPI , APP , Alzheimer disease amyloid protein , Amyloid precursor protein , Beta-amyloid precursor protein , Cerebral vascular amyloid peptide , CVAP , PreA4 , Protease nexin-II , PN-II

Protein function

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. / Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu2+ and Fe3+ to Cu+ and Fe2+, 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. Also binds GPC1 in lipid rafts. / 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).

Protein 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.

Involvement in disease

Alzheimer disease 1 (AD1) [MIM:104300]: 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. . Note: The disease is caused by mutations affecting the gene represented in this entry.; 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. . Note: The disease is caused by mutations affecting the gene represented in this entry.

Protein sequence and domain

The 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. / Belongs to the APP family. / Contains 1 BPTI/Kunitz inhibitor domain.

Protein post-translational modifications

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 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). Many other minor beta-amyloid peptides, beta-amyloid 1-X peptides, are found in cerebral spinal fluid (CSF) including the beta-amyloid X-15 peptides, produced from the cleavage by alpha-secretase and all terminatiing 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 beta-amyloid 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 beta-amyloid peptides (beta-amyloid 1-15, 1-16, 1-17, 1-18, 1-19 and 1-20) but not found on beta-amyloid 38, beta-amyloid 40 nor on beta-amyloid 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 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.

Protein cellular localization

Membrane; Single-pass type I membrane protein / Membrane > clathrin-coated pit

Research area

All research areas>Synthesis and Degradation>axin interactor 1
(View all antibody categories related to Synthesis and Degradation)

Note

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Supplier

St John’s Laboratory Ltd.

Product type

Primary antibody

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Immunofluorescence analysis of Rat lung tissue

1: Amyloid-beta Polyclonal Antibody(red) was diluted at 1:200 (4 degree Celsius,overnight).
2: Cy3 labled Secondary antibody was diluted at 1:300 (room temperature, 50min).
3: Picture B: DAPI(blue) 10min. Picture A:Target. Picture B: DAPI. Picture C: merge of A+B.
 

Immunofluorescence analysis of Rat lung tissue

1: Amyloid-beta Polyclonal Antibody(red) was diluted at 1:200 (4 degree Celsius,overnight).
2: Cy3 labled Secondary antibody was diluted at 1:300 (room temperature, 50min).
3: Picture B: DAPI(blue) 10min. Picture A:Target. Picture B: DAPI. Picture C: merge of A+B.
 

Immunofluorescence analysis of Mouse spleen tissue

1: Amyloid-beta Polyclonal Antibody(red) was diluted at 1:200 (4 degree Celsius,overnight).
2: Cy3 labled Secondary antibody was diluted at 1:300 (room temperature, 50min).
3: Picture B: DAPI(blue) 10min. Picture A:Target. Picture B: DAPI. Picture C: merge of A+B.
 

Immunofluorescence analysis of Mouse spleen tissue

1: Amyloid-beta Polyclonal Antibody(red) was diluted at 1:200 (4 degree Celsius,overnight).
2: Cy3 labled Secondary antibody was diluted at 1:300 (room temperature, 50min).
3: Picture B: DAPI(blue) 10min. Picture A:Target. Picture B: DAPI. Picture C: merge of A+B.
 

Immunohistochemical analysis of paraffin embedded Human liver tissue

1: Amyloid-beta Polyclonal Antibody was diluted at 1:200 (4 degree Celsius,overnight).
2: Sodium citrate pH 6.0 was used for antibody retrieval (>98 degree Celsius,20min).
3: Secondary antibody was diluted at 1:200 (room temperature, 30min). Negative control was used by secondary antibody only.
 

Immunohistochemical analysis of paraffin embedded Rat lung tissue

1: Amyloid-beta Polyclonal Antibody was diluted at 1:200 (4 degree Celsius,overnight).
2: Sodium citrate pH 6.0 was used for antibody retrieval (>98 degree Celsius,20min).
3: Secondary antibody was diluted at 1:200 (room temperature, 30min). Negative control was used by secondary antibody only.
 

Immunohistochemical analysis of paraffin embedded Rat kidney tissue

1: Amyloid-beta Polyclonal Antibody was diluted at 1:200 (4 degree Celsius,overnight).
2: Sodium citrate pH 6.0 was used for antibody retrieval (>98 degree Celsius,20min).
3: Secondary antibody was diluted at 1:200 (room temperature, 30min). Negative control was used by secondary antibody only.
 

Immunohistochemical analysis of paraffin embedded Rat spleen tissue

1: Amyloid-beta Polyclonal Antibody was diluted at 1:200 (4 degree Celsius,overnight).
2: Sodium citrate pH 6.0 was used for antibody retrieval (>98 degree Celsius,20min).
3: Secondary antibody was diluted at 1:200 (room temperature, 30min). Negative control was used by secondary antibody only.
 

Immunohistochemical analysis of paraffin embedded Mouse heart tissue

1: Amyloid-beta Polyclonal Antibody was diluted at 1:200 (4 degree Celsius,overnight).
2: Sodium citrate pH 6.0 was used for antibody retrieval (>98 degree Celsius,20min).
3: Secondary antibody was diluted at 1:200 (room temperature, 30min). Negative control was used by secondary antibody only.
 

Immunohistochemical analysis of paraffin embedded Mouse liver tissue

1: Amyloid-beta Polyclonal Antibody was diluted at 1:200 (4 degree Celsius,overnight).
2: Sodium citrate pH 6.0 was used for antibody retrieval (>98 degree Celsius,20min).
3: Secondary antibody was diluted at 1:200 (room temperature, 30min). Negative control was used by secondary antibody only.
 

Immunohistochemical analysis of paraffin embedded Mouse kidney tissue
1: Amyloid-¦Â Polyclonal Antibody was diluted at 1:200 (4 degree Celsius

1: Amyloid-beta Polyclonal Antibody was diluted at 1:200 (4 degree Celsius,overnight).
2: Sodium citrate pH 6.0 was used for antibody retrieval (>98 degree Celsius,20min).
3: Secondary antibody was diluted at 1:200 (room temperature, 30min). Negative control was used by secondary antibody only.


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