Skip to Content
Merck
All Photos(2)

Documents

P7854

Sigma-Aldrich

Anti-Presenilin-1 (S182) antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):

Anti-ACNINV3, Anti-AD3, Anti-FAD, Anti-PS-1, Anti-PS1, Anti-S182

Sign Into View Organizational & Contract Pricing


About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

mouse, human, Xenopus, rat

technique(s)

immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:100 using methacarn-fixed, formic acid-treated sections of Alzheimer′s Disease (AD) brain
microarray: suitable
western blot: 1:10,000 using whole cell extract of PC12 rat adrenal pheochromocytoma cell line

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... PSEN1(5663)
mouse ... Psen1(19164)
rat ... Psen1(29192)

General description

Presenilin 1& 2 (PS1 and PS2) are highly homologous proteins (approx. 43-52 kD) with eight transmembrane domains. In the brain, PS1 and PS2 are expressed primarily in neurons and localized mainly in cell bodies, axons and dendrites. In non-neuronal cells, PS1 and PS2 are localized to the nuclear membrane, endoplasmic reticulum and Golgi. Presenilin 1 is located on chromosome 14.

Specificity

Specific for presenilin 1 (not found in presenilin 2) and is identical in mouse, rat, and Xenopus. By immunoblotting, the antibody reacts with presenilin 1 (PS1, S182) and with the PS1 cleavage product.

Immunogen

synthetic peptide corresponding to the C-terminal of human presenilin-1 (amino acids 450-467 with N-terminally added lysine) conjugated to KLH.

Application

Anti-Presenilin-1 (S182) antibody produced in rabbit has been used in:
  • immunostaining
  • immunofluorescence detection
  • immunohistochemistry
  • immunoblotting

Biochem/physiol Actions

The biological functions of the presenilin′s are yet unknown, but they are thought to be involved in protein trafficking. Mutations in the presenilin 1 (PS1) gene (>30 known pathogenic mutations) have been found in about half of the early-onset familial Alzheimer′s disease (FAD), while only two pathogenic mutations have been found in PS2.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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.

Not finding the right product?  

Try our Product Selector Tool.

Storage Class Code

10 - Combustible liquids


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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

The presenilins
Tandon A and Fraser P
Genome Biology, 3(11) (2002)
The role of presenilins in Alzheimer?s disease
Thinakaran G
The Journal of Clinical Investigation, 104(10), 1321-1327 (1999)
Evangelos Konstantinidis et al.
Molecular therapy. Nucleic acids, 28, 450-461 (2022-05-05)
Presenilin 1 (PS1) is a central component of γ-secretase, an enzymatic complex involved in the generation of the amyloid-β (Aβ) peptide that deposits as plaques in the Alzheimer's disease (AD) brain. The M146L mutation in the PS1 gene (PSEN1) leads
Sara Massone et al.
The Journal of cell biology, 193(5), 851-866 (2011-06-01)
Alternative splicing generates protein isoforms that are conditionally or differentially expressed in specific tissues. The discovery of factors that control alternative splicing might clarify the molecular basis of biological and pathological processes. We found that IL1-α-dependent up-regulation of 38A, a
Silvia Di Loreto et al.
Experimental gerontology, 57, 57-65 (2014-05-20)
Although the beneficial responses induced in the central nervous system by early-initiated exercise have been broadly investigated, the effects of a chronic and moderate lately-initiated exercise on biochemical hallmarks of very early brain senescence have not been extensively studied. We

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service