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Key Documents

M3319

Sigma-Aldrich

Anti-Mint2 antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-Munc-18-1 Interacting Protein 2, Anti-X11β, Anti-X11L

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 120 kDa

species reactivity

rat

technique(s)

immunoprecipitation (IP): 5-10 μg using a rat brain extract (S1 fraction).
microarray: suitable
western blot: 0.25-0.5 μg/mL using rat brain extract (S1 fraction)

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... APBA2(321)
mouse ... Apba2(11784)
rat ... Apba2(83610)

Related Categories

General description

Munc-18-1 interacting protein 2 (Mint2), also called X11L, shares 50% homology with Mint1 and both are expressed exclusively in brain and bind Munc-18-1 with high affinity. It has N-terminal Munc-18-1-interacting domain (MID), a middle phosphotyrosine-binding (PTB) domain, and two C-terminal PDZ domain. It belongs to mammalian LIN-10 protein family. Mint 2 is present in neurons.

Immunogen

synthetic peptide corresponding to amino acids 1-18, located at the N-terminus of rat mint2, conjugated to KLH. This sequence is highly conserved (single amino acid substitution) in mouse mint2 and shows limited homology (66% identity) to human mint2. It does not share homology with the mint1 and mint3 isoforms.

Application

Anti-Mint2 antibody produced in rabbit has been used in:
  • immunoblotting
  • immunoprecipitation
  • immunostaining

Biochem/physiol Actions

Munc-18-1 interacting protein 2 (Mint2) participates in vesicle exocytosis. Mint 2 interacts with amyloid-β precursor protein (APP) and presenilins. It favors phosphorylation of β-amyloid precursor protein family members APP and Amyloid-like protein 2 (APLP2) in response to cellular stress, by facilitating c-Jun N-terminal kinase mediated phosphorylation.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% BSA and 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_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Mint proteins are required for synaptic activity-dependent amyloid precursor protein (APP) trafficking and amyloid $\beta$ generation
Sullivan S, et al.
The Journal of Biological Chemistry, 289(22), 15374-15383 (2014)
Regulation of APP-dependent transcription complexes by Mint/X11s: differential functions of Mint isoforms
Biederer T, et al.
The Journal of Neuroscience, 22(17), 7340-7351 (2002)
Intracellular amyloid precursor protein sorting and amyloid-$\beta$ secretion are regulated by Src-mediated phosphorylation of Mint2
Chaufty J, et al.
The Journal of Neuroscience, 32(28), 9613-9625 (2012)
Facilitation of stress-induced phosphorylation of beta-amyloid precursor protein family members by X11-like/Mint2 protein
Taru H and Suzuki T
Test, 279(20), 21628-21636 (2004)
Amy Y Lin et al.
Scientific reports, 9(1), 6024-6024 (2019-04-17)
MINT2/APBA2 is a synaptic adaptor protein involved in excitatory synaptic transmission. Several nonsynonymous coding variants in MINT2 have been identified in autism spectrum disorders (ASDs); however, these rare variants have not been examined functionally and the pathogenic mechanisms are unknown.

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