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Merck

N1660

Anti-Nicastrin antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonyme(s) :

Anti-ATAG1874

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A propos de cet article

UNSPSC Code:
12352203
NACRES:
NA.46
MDL number:
Conjugate:
unconjugated
Clone:
polyclonal
Application:
ARR, WB
Citations:
98
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biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 110 kDa

species reactivity

human, mouse, rat

enhanced validation

recombinant expression
Learn more about Antibody Enhanced Validation

technique(s)

microarray: suitable, western blot: 1:1,000 using minimum working antibody dilution using a whole cell extract of the HEK293 cell line stably transfected with human nicastrin.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... NCSTN(23385)

General description

Nicastrin (NCSTN) is a type I transmembrane glycoprotein (709 amino acids) that interacts with both presenilin-1 (PS1) and presenilin-2 (PS2). This gene is located on human chromosome 1q23.

Immunogen

synthetic peptide corresponding to the C-terminus of human nicastrin (amino acids 693-709) conjugated to KLH. The corresponding sequence is identical in mouse.

Application

Anti-Nicastrin antibody produced in rabbit has been used in:
  • western blotting
  • immunoprecipitation
  • co-immunoprecipitation

Biochem/physiol Actions

Nicastrin has a key role in the regulation of presenilin-mediated cleavage of the b-amyloid precursor protein (b-APP) and Notch/GLP-1. Nicastrin binds to the membrane-tethered form of Notch and is essential for the intramembrane cleavage of Notch to generate Notch intracellular domain (NICD), which is involved in intracellular signaling. It has been suggested that nicastrin binds substrates of presenilin/g-secretase complexes or modulates g-secretase activity. Suppression of nicastrin expression in C. elegansembryos induces a subset of notch/glp-1 phenotypes similar to those induced by simultaneous null mutations in both presenilin homologues of C. elegans (sel-12 and hop-1). Thus, increasing evidence indicates that both nicastrin and presenilins are necessary components for the intramembrane proteolysis of proteins such as b-APP and Notch, and implicates a direct role for nicastrin in the pathogenesis of Alzheimer′s disease and in the regulation of Notch signaling in vivo.
Rabbit polyclonal anti-Nicastrin recognizes human nicastrin (110 kDa) by immunoblotting. Staining of nicastrin in immunoblotting is specifically inhibited with nicastrin immunizing peptide.

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.


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Classe de stockage

10 - Combustible liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable



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Contenu apparenté

Instructions


Akio Fukumori et al.
The EMBO journal, 35(15), 1628-1643 (2016-05-26)
Intramembrane proteases execute fundamental biological processes ranging from crucial signaling events to general membrane proteostasis. Despite the availability of structural information on these proteases, it remains unclear how these enzymes bind and recruit substrates, particularly for the Alzheimer's disease-associated γ-secretase.
Keiro Shirotani et al.
The Journal of biological chemistry, 278(19), 16474-16477 (2003-03-20)
Gamma-secretase is a high molecular weight multicomponent protein complex with an unusual intramembrane-cleaving aspartyl protease activity. Gamma-secretase is intimately associated with Alzheimer disease because it catalyzes the proteolytic cleavage, which leads to the liberation of amyloid beta-peptide. At least presenilin
Aph-1 Associates Directly with Full-length and C-terminal Fragments of gamma-Secretase Substrates
Chen AC, et al.
The Journal of Biological Chemistry, 285(15), 11378-11391 (2010)