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Key Documents

MAB5556

Sigma-Aldrich

Anti-Nicastrin Antibody

ascites fluid, clone 9C3, Chemicon®

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

ascites fluid

antibody product type

primary antibodies

clone

9C3, monoclonal

species reactivity

rat, human, mouse

manufacturer/tradename

Chemicon®

technique(s)

immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable

isotype

IgG2b

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... NCSTN(23385)

Specificity

Nicastrin.

Immunogen

Synthetic peptide corresponding to the C terminal 18 a.a. of mouse Nicastrin. Due to sequence similarity, it is expected that the antibody will react with most mammals.

Application

Anti-Nicastrin Antibody is an antibody against Nicastrin for use in IP, WB & IC.
Western blot. The antibody recognizes a doublet of ~100-110 kDa. Suggested antibody dilution buffer is TBS with 0.1% Tween-20 and 5% non-fat milk powder. Suggested incubation time is overnight at 2-8°C or 1-2 hours at room temperature.

Immunocytochemistry

Immunoprecipitation. Suggested tissue/cell lysis buffer is 1% Triton X100 or 2% CHAPS. Suggested final reaction volume is 1000 μL with a final protein concentration in the reaction mix of 1 mg/mL. Suggested incubation time is overnight at 2-8°C with rotating. The antibody is known to co-precipitate in CHAPS: presenilin, Aph-1 and Pen-2. Optimal working dilutions must be determined by end user.

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Jolanta L Lundgren et al.
Journal of neurochemistry, 135(3), 606-615 (2015-08-25)
Synaptic degeneration and accumulation of the neurotoxic amyloid β-peptide (Aβ) in the brain are hallmarks of Alzheimer disease. Aβ is produced by sequential cleavage of the amyloid precursor protein (APP), by the β-secretase β-site APP cleaving enzyme 1 (BACE1) and
gamma-Secretase dependent production of intracellular domains is reduced in adult compared to embryonic rat brain membranes.
Fr?nberg, J; Karlstrom, H; Winblad, B; Tjernberg, LO; Frykman, S
Testing null
Rocío Pérez-González et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 34(9), 12922-12931 (2020-08-11)
Pleiotropic roles are proposed for brain extracellular vesicles (EVs) in the development of Alzheimer's disease (AD). Our previous studies have suggested a beneficial role for EVs in AD, where the endosomal system in vulnerable neurons is compromised, contributing to the
Ji-Yeun Hur et al.
The Journal of biological chemistry, 287(15), 11991-12005 (2012-02-09)
In Alzheimer disease, oligomeric amyloid β-peptide (Aβ) species lead to synapse loss and neuronal death. γ-Secretase, the transmembrane protease complex that mediates the final catalytic step that liberates Aβ from its precursor protein (APP), has a multitude of substrates, and
Mitsuhiro Inoue et al.
The FEBS journal, 282(14), 2587-2599 (2015-04-22)
The transmembrane protease complex γ-secretase is a key enzyme in Alzheimer disease pathogenesis as it liberates the neurotoxic amyloid β-peptide (Aβ); however, the mechanism of regulation of its activity in various cell types and subcellular compartments is largely unknown. Several

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