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MABN2295

Sigma-Aldrich

Anti-Amyloid beta A4 protein Antibody, clone 2E9

clone 2E9, from rat

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Synonym(s):
ABPP, APPI, APP, APP, Alzheimer disease amyloid protein, Amyloid precursor protein, Beta-amyloid precursor protein, Cerebral vascular amyloid peptide, CVAP, PreA4, Protease nexin-II, PN-II
eCl@ss:
32160702

biological source

rat

Quality Level

antibody form

purified antibody

antibody product type

primary antibodies

clone

2E9, monoclonal

species reactivity

mouse, human

technique(s)

immunofluorescence: suitable
immunoprecipitation (IP): suitable
western blot: suitable

isotype

IgG2aκ

NCBI accession no.

UniProt accession no.

shipped in

ambient

target post-translational modification

unmodified

Gene Information

human ... APP(351)

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MABN852

Anti-APP Antibody, clone 2B3

vibrant-m

ABN1641

Anti-APP585C

biological source

rat

biological source

rat

biological source

mouse

biological source

rabbit

Gene Information

human ... APP(351)

Gene Information

human ... APP(351)

Gene Information

human ... APP(351)

Gene Information

human ... APP(351)

clone

2E9, monoclonal

clone

2D8, monoclonal

clone

2B3, monoclonal

clone

polyclonal

antibody form

purified antibody

antibody form

purified antibody

antibody form

purified immunoglobulin

antibody form

serum

UniProt accession no.

P05067

UniProt accession no.

P05067

UniProt accession no.

P05067

UniProt accession no.

P05067

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General description

Amyloid beta A4 protein (UniProt: P05067; also known as ABPP, APPI. APP, APP, Alzheimer disease amyloid protein, Amyloid precursor protein, Beta-amyloid precursor protein, Cerebral vascular amyloid peptide, CVAP, PreA4, Protease nexin-II, PN-II) is encoded by the APP (also known as A4, AD1) gene (Gene ID: 351) in human. Deposition of Amyloid beta (Ab) is an early event in the pathogenesis of Alzheimer s disease (AD). Ab peptides originate from the proteolytic cleavage of the amyloid precursor protein (APP). APPs are cell surface protein that are 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. The beta-secretase cleaves APP between residues Met671 and Asp672 and yields sAPP beta and C99. Following the beta-secretase cleavage, a second cleavage occurs at the C-terminus of Ab peptide that releases Ab from C99. This cleavage occurs in the vicinity of residue 712 of the C-terminus. The gamma-secretase can cleave the C-terminal region at either Val711 or Ile713 to produce the shorter Ab peptide (Ab1-40) or the longer Ab peptide (Ab1-42). Ab1-42 occurs more frequently and forms fibrillar aggregates far more readily than the Ab1-40 peptide. 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. Abeta42 is a more effective reductant than beta-amyloid 40. From a physiological point of view, it functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. It is also involved in cell mobility and transcription regulation through protein-protein interactions and can promote transcription activation through binding to APBB1-KAT5.

Specificity

Clone 2E9 detects multiple isoforms of APP. It targets a sequence of 11 amino acids in the C-terminal region.

Immunogen

KLH-conjugated linear peptide corresponding to 11 amino acids from the C-terminal half of human Amyloid beta A4 protein (APP770).

Application

Anti-Amyloid beta A4 protein, clone 2E9 Antibody, Cat. No. MABN2295, is a highly specific rat monoclonal antibody that targets Amyloid beta A4 protein and has been tested in Immunofluorescence, Immunoprecipitation, and Western Blotting.
Research Category
Neuroscience
Western Blotting Analysis: 0.5 µg/mL from a representative lot detected Amyloid beta A4 protein in 10 µg of N2a, N2aA, and N2aAB cell lysate.

Immunofluorescence Analysis: A representative lot detected Amyloid beta A4 protein in Immunofluorescence applications (Willem, M., et. al. (2015). Nature. 526(7573):443-7).

Western Blotting Analysis: A representative lot detected Amyloid beta A4 protein in Western Blotting applications (Willem, M., et. al. (2015). Nature. 526(7573):443-7).

Immunoprecipitation Analysis: A representative lot detected Amyloid beta A4 protein in Immunoprecipitation applications (Willem, M., et. al. (2015). Nature. 526(7573):443-7).

Quality

Evaluated by Western Blotting in human Ntera-2 cell lysate.

Western Blotting Analysis: 0.5 ug/mL of this antibody detected Amyloid beta A4 protein in 10 µg of human Ntera-2 cell lysate

Target description

~110 kDa observed. Calculated 86.94 kDa for APP770, 78.66 kDa for APP695. Uncharacterized bands may be observed in some lysate(s).

Physical form

Format: Purified
Protein G purified
Purified rat monoclonal antibody IgG2a in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Storage and Stability

Stable for 1 year at 2-8°C from date of receipt.

Other Notes

Concentration: Please refer to lot specific datasheet.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Jichao Sun et al.
Nature communications, 10(1), 53-53 (2019-01-04)
CRISPR/Cas9 guided gene-editing is a potential therapeutic tool, however application to neurodegenerative disease models has been limited. Moreover, conventional mutation correction by gene-editing would only be relevant for the small fraction of neurodegenerative cases that are inherited. Here we introduce

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