N1660
Anti-Nicastrin antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
Synonym(s):
Anti-ATAG1874
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About This Item
Conjugate:
unconjugated
Clone:
polyclonal
Application:
ARR, WB
Citations:
98
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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Storage Class
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Related Content
Instructions
The Gene Encoding Nicastrin, a Major gamma-Secretase Component, Modifies Risk for Familial Early-Onset Alzheimer Disease in a Dutch Population-Based Sample
Dermaut B, et al.
American Journal of Human Genetics, 70, 1568-1574 (2002)
Yu Ohki et al.
Molecular neurodegeneration, 9, 7-7 (2014-01-15)
Amyloid-β peptide ending at 42nd residue (Aβ42) is believed as a pathogenic peptide for Alzheimer disease. Although γ-secretase is a responsible protease to generate Aβ through a processive cleavage, the proteolytic mechanism of γ-secretase at molecular level is poorly understood.
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.