MAB1563
Anti-Presenilin-1 Antibody, NT, clone hPS1-NT
culture supernatant, clone hPS1-NT, Chemicon®
Synonym(s):
Anti-ACNINV3, Anti-FAD, Anti-PS-1, Anti-PS1, Anti-S182
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All Photos(3)
About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
rat
Quality Level
antibody form
culture supernatant
antibody product type
primary antibodies
clone
hPS1-NT, monoclonal
species reactivity
human
manufacturer/tradename
Chemicon®
technique(s)
ELISA: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG2a
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... PSEN1(5663)
Related Categories
Specificity
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.
Immunogen
A fusion protein antigen containing the N-terminus of human PS-1 (residues 21-80) fused to GST.
Epitope: N-terminus
Application
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.
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
Neuroscience
Research Sub Category
Neurodegenerative Diseases
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.
Target description
32 kDa
Physical form
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
Storage and Stability
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.
Analysis Note
Control
Brain tissue
Brain tissue
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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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Description
Pricing
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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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
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
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
Claudia Marinangeli et al.
The Journal of biological chemistry, 290(11), 7169-7184 (2015-01-24)
Understanding the molecular mechanisms controlling the physiological and pathological activity of γ-secretase represents a challenging task in Alzheimer disease research. The assembly and proteolytic activity of this enzyme require the correct interaction of the 19 transmembrane domains (TMDs) present in
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