|Related Categories||Alphabetical Index, Antibodies, Antibodies for Alzheimer′s Disease, Antibodies for Neurobiology, Antibodies for Neurodegenerative Diseases Research,|
|species reactivity||human, mouse, rat|
|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.|
|antibody form||IgG fraction of antiserum|
|form||buffered aqueous solution|
|mol wt||antigen mol wt 110 kDa|
|shipped in||dry ice|
|Gene Information||human ... NCSTN(23385)|
synthetic peptide corresponding to the C-terminus of human nicastrin (amino acids 693-709) conjugated to KLH. The corresponding sequence is identical in mouse.
Nicastrin is a type I transmembrane glycoprotein (709 amino acids) that interacts with both presenilin-1 (PS1) and presenilin-2 (PS2). It 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.
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Rabbit polyclonal anti-Nicastrin is used to tag Nicastrin for detection and quantitation by immunocytochemical and immunohistochemical (IHC) techniques such as immunoblotting, immunoprecipitation, and immunofluorescence. It is used as a probe to determine the presence and roles of nicastrin in the regulation of presenilin-mediated cleavage of the β-amyloid precursor protein (b-APP) and Notch/GLP-1 (intramembrane proteolysis).
Alzheimer's disease (AD) is the most common cause of dementia in the elderly and is characterized by gradual loss of cognitive functions. Hallmark pathohistological findings of AD include widespread ...
Carolyn L. Crankshaw
BioFiles v7 n2, 2011, 4–8
Keywords: Alzheimer Disease, Gene expression, Genetic, Genetics, Inflammation, Metabolism, Phosphorylations
As a leading supplier of antibodies, Sigma® Life Science is committed to providing researchers the antibody they need with the quality they deserve. Our Antibody Explorer Search Tool provides easy ac...
Keywords: Buffers, Cell biology, Epigenetics, Immunohistochemistry, Immunoprecipitation, Molecular biology, Neuroscience, Western blot
Functional analysis of the transmembrane domains of presenilin 1: participation of transmembrane domains 2 and 6 in the formation of initial substrate-binding site of gamma-secretase. Watanabe, N., et al. J. Biol. Chem. 285, 19738-46, (2010)
The large hydrophilic loop of presenilin 1 is important for regulating gamma-secretase complex assembly and dictating the amyloid beta peptide (Abeta) Profile without affecting Notch processing. Wanngren, J., et al. J. Biol. Chem. 285, 8527-36, (2010)
CD147, a gamma-secretase associated protein is upregulated in Alzheimer's disease brain and its cellular trafficking is affected by presenilin-2. Nahalkova, J., et al. Neurochem. Int. 56, 67-76, (2010)
Polar transmembrane-based amino acids in presenilin 1 are involved in endoplasmic reticulum localization, Pen2 protein binding, and γ-secretase complex stabilization. Fassler, M., et al. J. Biol. Chem. 286, 38390-6, (2011)
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