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Merck
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MAB348-AF555

Anti-APP A4 Antibody, a.a. 66-81 of APP {NT}, clone 22C11, Alexa Fluor 555

clone 22C11, from mouse, ALEXA FLUOR 555

别名:

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

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关于此项目

UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Conjugate:
ALEXA FLUOR 555
Clone:
22C11, monoclonal
Application:
ICC
Citations:
-
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biological source

mouse

conjugate

ALEXA FLUOR 555

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

22C11, monoclonal

species reactivity

canine, human, mouse, rat, porcine, monkey, fish

technique(s)

immunocytochemistry: suitable

isotype

IgG1

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Quality Level

Gene Information

human ... APP(351)

General description

Amyloid beta A4 protein (UniProt P05067; also known as ABPP, Alzheimer disease amyloid protein, Amyloid precursor protein, APP, APPI, Cerebral vascular amyloid peptide, CVAP, PN-II, PreA4, Protease nexin-II) is encoded by the APP (also known as A4, AD1) gene (Gene ID 351) in human. Amyloid precursor protein (APP) is initially produced with a signal peptide sequence (a.a. 1-17), the removal of which yields the mature protein with a large extracellular portion (a.a. 18-699), followed by a transmembrane segment (a.a. 700-723) and a cytoplasmic (a.a. 724-770) tail. APP can be further processed by the α-, β-, and γ-secretases in two alternative processing pathways. In the non-amyloidogenic pathway, APP is first cleaved by the plasma membrane-localized α-secretase to generate an N-terminal extracellular sAPPα fragment (a.a. 18-687) and a membrane-bound C-terminal fragment C83 (CTFα), which can be further cleaved by γ-secretase to produce a non-toxic small peptide p3 and a cytoplasmic APP intracellular domain (AICD). In the amyloidogenic pathway, APP undergoes β-cleavage in BACE-1 (β-site APP-cleaving enzyme)-enriched endosomes to generate an N-terminal extracellular sAPPβ fragment (a.a. 18-671) and a membrane-bound C-terminal fragment C99 (CTFβ). Subsequent cleavage of C99 by γ-secretase releases the amyloid β peptide (Aβ) and AICD. Aβ accumulation in the cortical and hippocampal regions of the brain is a major pathological feature of Alzheimer′s disease (AD).
~110/120/130 kDa observed.

Immunogen

Epitope: Amino acids 66-81 of APP.
Purified recombinant Alzheimer precursor A4 (pre-A4695) fusion protein.

Application

Anti-APP A4 Antibody, a.a. 66-81 of APP {NT}, clone 22C11, Alexa Fluor 555 is an antibody against APP A4 for use in Immunocytochemistry.
Research Category
Neuroscience
Research Sub Category
Neurodegenerative Diseases
The unconjugated antibody (Cat. No. MAB348) is shown to be suitable also for immunohistochemistry (for both frozen and paraffin-embedded sections), immunofluorescence, and Western blotting applications.

Biochem/physiol Actions

Clone 22C11 reacts with pre-A4. The antibody recognizes amino acids 66-81 of the N-terminus on the pre-A4 molecule (Hilbich, C., et al. (1993). J. Biol. Chem. 268(35):26571-26577). Clone 22C11 recognizes all three isoforms of APP, immature ~110kDa, sAPP ~120kDa, and mature ~130kDa (Hoffmann, J., et al. (2000). Eur. J. Cell. Biol.79(12):905-914.). The antibody is known to cross react with APLP2 (Slunt, H.H., et al. (1994). J. Biol. Chem. 269(4):2637-2644).

Physical form

Protein A purified
Purified mouse monoclonal IgG1 antibody conjugate in PBS with 15 mg/mL BSA and 0.1 % sodium azide.

Preparation Note

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

Analysis Note

Evaluated by Immunocytochemistry in SH-5YSY cells.

Immunocytochemistry Analysis: A 1:100 dilution of this antibody detected APP A4 in SH-5YSY cells.

Other Notes

Concentration: Please refer to lot specific datasheet.

Legal Information

ALEXA FLUOR is a trademark of Life Technologies

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.

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存储类别

12 - Non Combustible Liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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相关内容

Alzheimer’s Disease is a progressively deteriorating disease. It manifests itself with memory loss, confusion, problems with judgment, planning, concentration, and personality changes; and in it’s later stages, a decline in physical abilities. The disease’s causes, cures, and preventions are unknown; however, key proteins likely involved in the degenerative mechanism have been identified. Alzheimer’s Disease is characterized by neuronal loss, alterations in neurotransmitter systems, and the presence of neurofibrillary tangles composed of abnormally hyperphosphorylated tau proteins. A prominent feature of Alzheimer’s Disease is the formation of senile plaques in selected regions of the brain. The center of these plaques are composed mainly of fibrillary aggregates of a common, but not well understood, b amyloid peptides (Aβ). The Aβ peptides are generated from the larger amyloid-β precursor protein (APP) by the sequential action of β- and γ-secretase, and it is generally accepted that oligomeric forms of this Aβ are neurotoxic, resulting in disease progression.

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