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MABN639

Sigma-Aldrich

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

clone 1E8, 1 mg/mL, from mouse

Sinônimo(s):

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

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About This Item

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

fonte biológica

mouse

Nível de qualidade

forma do anticorpo

affinity purified immunoglobulin

tipo de produto de anticorpo

primary antibodies

clone

1E8, monoclonal

purificado por

affinity chromatography

reatividade de espécies

human

concentração

1 mg/mL

técnica(s)

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

Isotipo

IgG1κ

nº de adesão UniProt

Condições de expedição

wet ice

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... APP(351)

Descrição geral

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.

Especificidade

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

Imunogênio

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

Aplicação

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.

Qualidade

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.

Descrição-alvo

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

forma física

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

Armazenamento e estabilidade

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.

Exoneração de responsabilidade

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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Pictogramas

Skull and crossbones

Palavra indicadora

Danger

Frases de perigo

Classificações de perigo

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

Código de classe de armazenamento

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

Classe de risco de água (WGK)

WGK 1


Certificados de análise (COA)

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Urea-based two-dimensional electrophoresis of beta-amyloid peptides in human plasma: evidence for novel Abeta species.
Maler, JM; Klafki, HW; Paul, S; Spitzer, P; Groemer, TW; Henkel, AW; Esselmann et al.
Proteomics null
gamma-Secretase heterogeneity in the Aph1 subunit: relevance for Alzheimer's disease.
Serneels, L; Van Biervliet, J; Craessaerts, K; Dejaegere, T; Horre, K; Van Houtvin et al.
Science (New York, N.Y.) null
J Wiltfang et al.
The Journal of biological chemistry, 276(46), 42645-42657 (2001-08-30)
Urea-based beta-amyloid (Abeta) SDS-polyacrylamide gel electrophoresis and immunoblots were used to analyze the generation of Abeta peptides in conditioned medium from primary mouse neurons and a neuroglioma cell line, as well as in human cerebrospinal fluid. A comparable and highly
Highly conserved and disease-specific patterns of carboxyterminally truncated Abeta peptides 1-37/38/39 in addition to 1-40/42 in Alzheimer's disease and in patients with chronic neuroinflammation.
Wiltfang, J; Esselmann, H; Bibl, M; Smirnov, A; Otto, M; Paul, S; Schmidt, B; Klafki et al.
Journal of Neurochemistry null
Christopher P Sullivan et al.
Neurobiology of disease, 43(2), 338-345 (2011-04-26)
Retromer deficiency has been implicated in sporadic AD and animals deficient in retromer components exhibit pronounced neurodegeneration. Because retromer performs retrograde transport from the endosome to the Golgi apparatus and neuronal Aβ is found in late endosomal compartments, we speculated

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