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安全信息

MABN2287

Sigma-Aldrich

Anti-APP Antibody, clone 1D1

clone 1D1, from rat

别名:

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

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About This Item

UNSPSC代码:
12352203
eCl@ss:
32160702
NACRES:
NA.41

生物来源

rat

质量水平

抗体形式

purified immunoglobulin

抗体产品类型

primary antibodies

克隆

1D1, monoclonal

种属反应性

human

技术

ELISA: suitable
flow cytometry: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable (paraffin)
western blot: suitable

同位素/亚型

IgG1κ

NCBI登记号

UniProt登记号

运输

ambient

靶向翻译后修饰

unmodified

基因信息

human ... APP(351)

一般描述

Amyloid beta A4 protein (UniProt: P05067; also known as 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) is encoded by the APP (also known as A4, AD1) gene (Gene ID: 351) in human. APP undergoes extensive post-translational modification including glycosylation, phosphorylation, and tyrosine sulfation, as well as many types of proteolytic processing to generate peptide fragments. APP is proteolytically processed under normal cellular conditions by alpha-secretase or beta-secretase to generate and release 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. In Alzheimer s disease processing of C99 generates amyloid-beta 40 (Abeta40) and amyloid-beta 42 (Abeta42) that form amyloid plaques. Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. They bind transient metals such as copper, zinc and iron. APP can also be 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. In addition to its obvious role in Alzheimer′s disease, the most-substantiated role for APP is in synaptic formation and repair. Its expression is upregulated during neuronal differentiation and after neural injury. Clone 1D1 is shown to bind to the N-terminus of APP and detects both the soluble full length and secreted hAPP and can also detect transgenic APP expression in APP-transgenic animal models.

特异性

Clone 1D1 specifically detects human amyloid precursor protein (APP) and does not display reactivity with other species. It targets an epitope within the ectodomain region of APP and does not react with A beta peptide.

免疫原

StrepII-tagged human recombinant ectodomain region of the neuronal isoform of hAPP695 lacking the KPI domain.

应用

Anti-APP, clone 1D1, Cat. No. MABN2287, is a highly specific rat monoclonal antibody that targets Amyloid beta A4 protein and has been tested for use in ELISA, Flow Cytometry, Immunocytochemistry, Immunohistochemistry (Paraffin), and Western Blotting.
Note: For the Western blotting application use of nitocellulose is highly recommended and the samples must be boiled in non-reduing laemmli buffer. Please note that clone 1D1 recognizes APP only in its quasi-native folded form.

Immunoprecipitation Analysis: A representative lot detected APP in Immunoprecipitation applications (Hofling, C., et. al. (2016). Aging Cell. 15(5):953-63).

Western Blotting Analysis: A representative lot detected APP in WT, but not in APP knockdown HEK293T cells (Courtesy of Dr. med. Peer-Hendrik Kuhn, Ph.D., Institut fur Allgemeine Pathologie und Pathologische Anatomie, Technische Universität München, Munich, Germany).

Immunocytochemistry Analysis: A 1:250 dilution from a representative lot detected APP in HEK293 cell line.

Immunocytochemistry Analysis: A representative lot detected APP in Immunocytochemistry applications (Hofling, C., et. al. (2016). Aging Cell. 15(5):953-63).

Immunocytochemistry Analysis: A 1:10 dilution from a representative lot detected APP in HEK293T cells, but not in cells lentivirally transduced with APP shRNA-1 or APP shRNA-2, both coexpressing GFP as a reporter (Courtesy of Dr. med. Peer-Hendrik Kuhn, Ph.D., Institut fur Allgemeine Pathologie und Pathologische Anatomie, Technische Universität München, Munich, Germany).

Immunohistochemistry Analysis: A representative lot detected APP in Immunohistochemistry applications (Hofling, C., et. al. (2016). Aging Cell. 15(5):953-63).

Immunohistochemistry Analysis: A 1:50 dilution from a representative lot detected APP in human cerebral cortex and human Alzheimer′s brain tissues.

ELISA Analysis: A representative lot detected APP in ELISA applications (Hofling, C., et. al. (2016). Aging Cell. 15(5):953-63).

Western Blotting Analysis: A representative lot detected APP in Western Blotting applications (Hofling, C., et. al. (2016). Aging Cell. 15(5):953-63).

Flow Cytometry Analysis: A representative lot detected APP in Flow Cytometry applications (Hofling, C., et. al. (2016). Aging Cell. 15(5):953-63).
Research Category
Neuroscience

质量

Evaluated by Western Blotting in HEK293 cell lysate.

Western Blotting Analysis: 1 µg/mL of this antibody detected APP in 10 µg of HEK293 cell lysate.

目标描述

~100 kDa observed; 86.94 kDa calculated. Uncharacterized bands may be observed in some lysate(s).

外形

Protein G purified
Format: Purified
Purified rat monoclonal antibody IgG1 in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

储存及稳定性

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

其他说明

Concentration: Please refer to lot specific datasheet.

免责声明

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.

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Andrew Octavian Sasmita et al.
Nature neuroscience, 27(9), 1668-1674 (2024-08-06)
Amyloid-β (Aβ) is thought to be neuronally derived in Alzheimer's disease (AD). However, transcripts of amyloid precursor protein (APP) and amyloidogenic enzymes are equally abundant in oligodendrocytes (OLs). By cell-type-specific deletion of Bace1 in a humanized knock-in AD model, APPNLGF

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