Ugrás a tartalomra
Merck

A8326

Sigma-Aldrich

Anti-β-Amyloid Protein (1-40) antibody produced in rabbit

enhanced validation

whole antiserum

Szinonimák:

Anti-AAA, Anti-ABETA, Anti-ABPP, Anti-AD1, Anti-APPI, Anti-CTFgamma, Anti-CVAP, Anti-PN-II, Anti-PN2, Anti-alpha-sAPP, Anti-preA4

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

MDL-szám:
UNSPSC kód:
12352203
NACRES:
NA.41
konjugátum:
unconjugated
application:
ELISA (i)
IHC (p)
klón:
polyclonal
faj reaktivitás:
human
citations:
14
technika/technikák:
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:100 using human Alzheimer’s disease (AD) brain tissue
indirect ELISA: 1:4000-1:8000

biológiai forrás

rabbit

Minőségi szint

konjugátum

unconjugated

antitest forma

whole antiserum

antitest terméktípus

primary antibodies

klón

polyclonal

Forma

liquid

tartalmaz

15 mM sodium azide

faj reaktivitás

human

fejlettebb validálás

independent
Learn more about Antibody Enhanced Validation

technika/technikák

immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:100 using human Alzheimer’s disease (AD) brain tissue
indirect ELISA: 1:4000-1:8000

UniProt elérési szám

kiszállítva

dry ice

tárolási hőmérséklet

−20°C

célzott transzláció utáni módosítás

unmodified

Géninformáció

human ... APP(351)

Általános leírás

Amyloid precursor proteins (APPs) are members of a large family of 70 kDa transmembrane glycoproteins that are found in a wide range of tissues. APP is expressed in the brain. It is located on human chromosome 21. APPs have three main isoforms, namely, APP695, APP751 and APP770, that are derived from alternative splicing events in cells.

Immunogén

synthetic β-amyloid (1-40) conjugated to BSA.

Alkalmazás

Anti-β-Amyloid Protein (1-40) antibody produced in rabbit has been used in:
  • immunocytochemical localization of Aβ peptides
  • immunocytochemistry
  • immunoprecipitation
  • focused ultrasound-microbubble enhanced antibody delivery (FUS-MB)

Biokémiai/fiziológiai hatások

The β-amyloid precursor protein (APP) is cleaved sequentially by the proteolytic enzymes β-secretase (BACE1) and γ-secretase to produce β-amyloid (Aβ) peptides with the Aβ1-42 and the Aβ1-40 forms being the most prevalent. Secreted Aβ peptides are degraded either via a re-uptake mechanism followed by endosomal degradation, or by an extracellular insulin degrading enzyme. Extracellular accumulation of Aβ leads to the formation of aggregates, fibrils and eventually amyloid deposits called neuritic plaques, which is the hallmark of Alzheimer′s disease (AD).
Rabbit Anti-β-Amyloid Protein (1-40) antibody does not stain control sections of normal brain tissues.

Fizikai forma

Rabbit Anti-β-Amyloid (1-40) is supplied as a liquid containing 0.1% sodium azide as preservative.

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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Tárolási osztály kódja

10 - Combustible liquids

WGK

WGK 3

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


Válasszon a legfrissebb verziók közül:

Analitikai tanúsítványok (COA)

Lot/Batch Number

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

Dokumentumtár megtekintése

Scott B Raymond et al.
PloS one, 3(5), e2175-e2175 (2008-05-15)
Alzheimer's disease is a neurodegenerative disorder typified by the accumulation of a small protein, beta-amyloid, which aggregates and is the primary component of amyloid plaques. Many new therapeutic and diagnostic agents for reducing amyloid plaques have limited efficacy in vivo
Yanfang Rui et al.
Molecular brain, 9(1), 79-79 (2016-08-19)
Small oligomeric forms of amyloid-β (Aβ) are believed to be the culprit for declined brain functions in AD in part through their impairment of neuronal trafficking and synaptic functions. However, the precise cellular actions of Aβ oligomers and underlying mechanisms
Jhana O Hendrickx et al.
International journal of molecular sciences, 22(13) (2021-07-03)
Increasing epidemiological evidence highlights the association between systemic insulin resistance and Alzheimer's disease (AD). As insulin resistance can be caused by high-stress hormone levels and since hypercortisolism appears to be an important risk factor of AD, we aimed to investigate
Learning performances, brain NGF distribution and NPY levels in transgenic mice expressing TNF-alpha
Fiore M, et al.
Behavioural Brain Research, 112(1), 165-175 (2000)
S Benjannet et al.
The Journal of biological chemistry, 276(14), 10879-10887 (2001-01-22)
Processing of the beta-amyloid precursor protein (betaAPP) by beta- and gamma-secretases generates the amyloidogenic peptide Abeta, a major factor in the etiology of Alzheimer's disease. Following the recent identification of the beta-secretase beta-amyloid-converting enzyme (BACE), we herein investigate its zymogen

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