P7854

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

Name: Anti-Presenilin-1 (S182) antibody produced in rabbit
Brand: SIGMA

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):

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

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All Photos(2)

About This Item

UNSPSC Code:

12352203

NACRES:

NA.41

MDL number:

MFCD02097229

Product Name

Anti-Presenilin-1 (S182) antibody produced in rabbit, IgG fraction of antiserum, buffered aqueous solution

Quality Level

200

biological source

rabbit

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.

P49768

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

Application

Anti-Presenilin-1 (S182) antibody produced in rabbit has been used in:

immunostaining
immunofluorescence detection
immunohistochemistry
immunoblotting

Biochem/physiol Actions

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.

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.

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.

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.

Immunogen

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

Physical form

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

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Storage Class

10 - Combustible liquids

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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)

CRISPR-Cas9 treatment partially restores amyloid-β 42/40 in human fibroblasts with the Alzheimer's disease PSEN 1 M146L mutation.

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

RNA polymerase III drives alternative splicing of the potassium channel-interacting protein contributing to brain complexity and neurodegeneration.

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

Regular and moderate exercise initiated in middle age prevents age-related amyloidogenesis and preserves synaptic and neuroprotective signaling in mouse brain cortex.

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

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