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Merck
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MABN639

Sigma-Aldrich

Anti-Amyloid βA4, clone 1E8 (Amino Terminus) Antibody

clone 1E8, 1 mg/mL, from mouse

Szinonimák:

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

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

UNSPSC kód:
12352203
eCl@ss:
32160702
NACRES:
NA.41
klón:
1E8, monoclonal
application:
IHC
IP
WB
faj reaktivitás:
human
technika/technikák:
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
citations:
3

biológiai forrás

mouse

Minőségi szint

antitest forma

affinity purified immunoglobulin

antitest terméktípus

primary antibodies

klón

1E8, monoclonal

tisztítva

affinity chromatography

faj reaktivitás

human

koncentráció

1 mg/mL

technika/technikák

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

izotípus

IgG1κ

UniProt elérési szám

kiszállítva

wet ice

célzott transzláció utáni módosítás

unmodified

Géninformáció

human ... APP(351)

Általános leírás

Amyloid beta A4 protein, also known as ABPP or APPI (APP) or Alzheimer disease amyloid protein or Cerebral vascular amyloid peptide (CVAP) or PreA4 or Protease nexin-II (PN-II), and encoded by the gene name APP or A4 or AD1, belongs to the APP family. The beta-amyloid peptide (beta A4), proteolytically released from the amyloid precursor protein (APP), is the principal component of senile plaques in Alzheimer′s disease. Cleavage of APP by alpha-secretase or alternatively by beta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, respectively, and the retention of corresponding membrane-anchored C-terminal fragments, C83 and C99. Subsequent processing of C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is nonamyloidogenic. 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). Mab βA4N-1E8 recognizes the free N-terminus of the bA4 polypeptide with high preference and crossreacts with sAPPα.

Egyediség

This antibody is specific for the first 2 amino acids of the Amyloid beta peptide amino terminus.

Immunogén

Epitope: N-terminus
KLH-conjugated peptide corresponding to the N-terminus of human Amyloid βA4.

Alkalmazás

Immunohistochemistry Analysis: A 1:500-2,000 dilution from a representative lot was used to detect Amyloid βA4 in human Alzheimer′s brain and thalamus tissues.

Western Blotting Analysis: A representative lot was used to detect Amyloid βA4 in Western Blotting. (Wiltfang, et al. 2001; Serneels, et al. 2009; Maler, et al. 2007).

Immunoprecipitation Analysis: A representative lot was used to detect Amyloid βA4 in Immunoprecipitation. (Wiltfang, et al. 2001; Maler, et al. 2007).
Research Category
Neuroscience
Research Sub Category
Neurodegenerative Diseases
This Anti-Amyloid βA4, clone 1E8 (Amino Terminus) Antibody is validated for use in western blotting, IHC & IP for the detection of Amyloid βA4.

Minőség

Evaluated by Western Blotting in human Alzheimer′s brain tissue lysate.

Western Blotting Analysis: A 1:1,000 dilution of this antibody detected Amyloid βA4 in human Alzheimer′s brain tissue lysate.

Cél megnevezése

~4 kDa observed. Uncharacterized bands may be observed in some lysate(s).

Fizikai forma

Affinity
Purified mouse monoclonal IgG1κ in buffer containing PBS, PEG, Sucrose, and up to 0.1% sodium azide.

Tárolás és stabilitás

For long-term storage, freeze lyophilizate upon arrival (2-8°C). Upon reconstitution, aliquote and freeze in liquid nitrogen; reconstituted antibody can be stored frozen at -80°C up to 1 year. Thaw aliquots at 37°C. Thawed aliquots may be stored at 4°C up to 3 months.

Avoid repeated freeze / thaw cycles.

Jogi nyilatkozat

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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Piktogramok

Skull and crossbones

Figyelmeztetés

Danger

Figyelmeztető mondatok

Veszélyességi osztályok

Acute Tox. 3 Dermal - Acute Tox. 4 Inhalation - Acute Tox. 4 Oral - Aquatic Chronic 3

Tárolási osztály kódja

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

WGK

WGK 1


Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

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Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.

Dokumentumtár megtekintése

Lauren H Fairley et al.
Proceedings of the National Academy of Sciences of the United States of America, 120(8), e2209177120-e2209177120 (2023-02-15)
Microglial phagocytosis is an energetically demanding process that plays a critical role in the removal of toxic protein aggregates in Alzheimer's disease (AD). Recent evidence indicates that a switch in energy production from mitochondrial respiration to glycolysis disrupts this important
Daniela Giraldo-Berrio et al.
Neurotoxicity research, 42(3), 28-28 (2024-06-06)
Parkinson's disease with dementia (PDD) is a neurological disorder that clinically and neuropathologically overlaps with Parkinson's disease (PD) and Alzheimer's disease (AD). Although it is assumed that alpha-synuclein ( α -Syn), amyloid beta (A β ), and the protein Tau
Nicolas Gomez-Sequeda et al.
International journal of molecular sciences, 25(9) (2024-05-11)
Familial Alzheimer's disease (FAD) is a complex and multifactorial neurodegenerative disorder for which no curative therapies are yet available. Indeed, no single medication or intervention has proven fully effective thus far. Therefore, the combination of multitarget agents has been appealing

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