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Merck
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MAB1563

Sigma-Aldrich

Anti-Presenilin-1 Antibody, NT, clone hPS1-NT

culture supernatant, clone hPS1-NT, Chemicon®

Szinonimák:

Anti-ACNINV3, Anti-FAD, Anti-PS-1, Anti-PS1, Anti-S182

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

UNSPSC kód:
12352203
eCl@ss:
32160702
NACRES:
NA.41
klón:
hPS1-NT, monoclonal
application:
ELISA
IHC
IP
WB
faj reaktivitás:
human
technika/technikák:
ELISA: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
citations:
44

biológiai forrás

rat

Minőségi szint

antitest forma

culture supernatant

antitest terméktípus

primary antibodies

klón

hPS1-NT, monoclonal

faj reaktivitás

human

gyártó/kereskedő neve

Chemicon®

technika/technikák

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

izotípus

IgG2a

NCBI elérési szám

UniProt elérési szám

kiszállítva

wet ice

célzott transzláció utáni módosítás

unmodified

Géninformáció

human ... PSEN1(5663)

Egyediség

Recognizes Presenilin-1, human. By Western blot the antibody recognizes a predominant 32 kDa polypeptide in a variety of samples, including PC12 cells transfected with human PS1 complementary DNA, brain biopsy specimens from demented patients, and postmortem samples of frontal neucortex from Familial Alzheimer′s Disease cases, late-onset Alzheimer′s disease cases, and cases of other degenerative disorders. Immunohistochemical studies of control brains revealed that PS1 is expressed primarily in neurons, with the protein localizing in the soma and dendritic processes. In contrast in FAD and sporadic Alzheimer′s disease cases, PS1 immunoreactivity was present in the neuritic component of senile plaques as well as in neurofibrillary tangles. Localization of PS1 immunoreactivity in familial and sporadic Alzheimer′s disease suggest that genetically heterogeneous forms of the disease share a common pathophysiology involving PS1 protein.

Immunogén

A fusion protein antigen containing the N-terminus of human PS-1 (residues 21-80) fused to GST.
Epitope: N-terminus

Alkalmazás

Immunohistochemistry: rat pups and 24 old month rats were perfused for 10 minutes with 100-200mL of 4% PFA 0.3% glutaraldehyde and 0.1% CaCl2 in 0.1M PBS pH 7.4. Vibratome sections were blocked with 3% normal serum and permeabilized with 0.1% triton X-100.{Neuroscience 2003 120:405-423}.

Immunoblotting: 1:250-1:500. Recommend blocking buffer is TBS containing 5% non fat milk and 0.01% Tween 20. It is recommended that you also dilute the antibody in this blocking buffer. Incubate with the MAB1563 for 1 to 2 hours at room temperature or overnight at 4°C.

Immunoprecipitation

ELISA

Optimal working dilutions must be determined by end user.
Research Category
Neuroscience
Research Sub Category
Neurodegenerative Diseases
This Anti-Presenilin-1 Antibody, N-terminus, clone hPS1-NT is validated for use in ELISA, IH, IP, WB for the detection of Presenilin-1.

Cél megnevezése

32 kDa

Fizikai forma

UnPurified mouse tissue culture supernatant from a perfusion system, filtered through a 0.2μ micron membrane prior to vialing. Product contains 20%FBS and Ciprofloxacin at final concentration of 10μg/mL.
Unpurified

Tárolás és stabilitás

Maintain for 1 year at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

Analízis megjegyzés

Control
Brain tissue

Egyéb megjegyzések

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Jogi információk

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

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 1

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


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.

Már rendelkezik ezzel a termékkel?

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

Dokumentumtár megtekintése

Lindsay Poppe et al.
Alzheimer's research & therapy, 11(1), 102-102 (2019-12-14)
EphA4 is a receptor of the ephrin system regulating spine morphology and plasticity in the brain. These processes are pivotal in the pathophysiology of Alzheimer's disease (AD), characterized by synapse dysfunction and loss, and the progressive loss of memory and
Sun Young Oh et al.
Journal of neurochemistry, 113(1), 262-274 (2010-01-22)
The amyloid precursor protein is a ubiquitously expressed transmembrane protein that has been long implicated in the pathogenesis of Alzheimer's disease but its normal biological function has remained elusive despite extensive effort. We have previously reported the identification of Notch2
Nuomin Li et al.
Frontiers in aging neuroscience, 8, 51-51 (2016-03-26)
Alzheimer disease (AD) is characterized by progressive memory loss, reduction in cognitive functions, and damage to the brain. The β-amyloid precursor protein can be sequentially cleaved by β- secretase and γ-secretase. Mutations in the presenilin1(PS1) are the most common cause
Hermeto Gerber et al.
Acta neuropathologica communications, 7(1), 13-13 (2019-02-02)
The adipocyte plasma membrane-associated protein APMAP is expressed in the brain where it associates with γ-secretase, a protease responsible for the generation of the amyloid-β peptides (Aβ) implicated in the pathogenesis of Alzheimer's disease (AD). In this study, behavioral investigations
Marty A Fernandez et al.
The Journal of biological chemistry, 289(45), 31043-31052 (2014-09-23)
The presenilin-containing γ-secretase complex produces the amyloid β-peptide (Aβ) through intramembrane proteolysis, and >100 presenilin mutations are associated with familial early-onset Alzheimer disease (AD). The question of whether these mutations result in AD through a gain or a loss of

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