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Key Documents

M3194

Sigma-Aldrich

Anti-Mint1 antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):

Anti-Munc-18-1 Interacting Protein 1, Anti-X11α, Anti-mLin-10

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About This Item

MDL number:
UNSPSC Code:
12352203

biological source

rabbit

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 120 kDa

species reactivity

rat, mouse

technique(s)

immunoprecipitation (IP): 10-20 μL using rat brain extract (S1 fraction)
western blot: 1:1,000-1:2,000 using rat brain and a mouse brain extract (S1 fraction)

UniProt accession no.

shipped in

dry ice

Storage temp.

−20°C

Gene Information

mouse ... Apba1(319924)
rat ... Apba1(83589)

Immunogen

synthetic peptide corresponding to amino acids 1-19 located at the N-terminus of rat mint1. The sequence is highly conserved (90% identity) in human mint1. It does not share homology with the mint2 and mint3 isoforms.

Target description

Mint1 a member of the X11 protein family. It is a neuronal adapter protein that interacts with the Alzheimer′s disease amyloid precursor protein (APP). It stabilizes APP and inhibits production of proteolytic APP fragments including the A beta peptide tha

Physical form

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

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Y Nakajima et al.
Brain research. Molecular brain research, 92(1-2), 27-42 (2001-08-03)
Mints are multimodular adapter proteins in functioning membrane transport and organization. Mint1 and mint2 are neuron-specific. We localized these isoforms in mouse brain. By in situ hybridization, mRNA encoding mint1 or mint2 was expressed in neurons throughout the brain. Mint1
Thomas Biederer et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 22(17), 7340-7351 (2002-08-28)
Mints/X11s are neuron-specific (Mints 1 and 2) and ubiquitous (Mint 3) adaptor proteins composed of isoform-specific N-terminal sequences and common C-terminal phosphotyrosine-binding (PTB) and PDZ domains. We now show that all three Mints bind to the cytoplasmic tail of amyloid-beta

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