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Merck

A8530

Sigma-Aldrich

m-Aminophenylboronic acid–Agarose

saline suspension

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About This Item

MDL number:
UNSPSC Code:
12161501
PubChem Substance ID:
NACRES:
NA.32

form

saline suspension

Quality Level

extent of labeling

5-20 μmol per mL

matrix

cross-linked 6% beaded agarose

matrix activation

epoxy

matrix attachment

amino

matrix spacer

12 atoms

storage temp.

2-8°C

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General description

m-Aminophenylboronic acid–Agarose is applicable as a boronate affinity matrix for the purification of severe acute respiratory syndrome′s (SARS-CoV) nucleoprotein (NP) antigen.

Application

m-Aminophenylboronic acid–Agarose has been used as a separating gel in the boronate affinity chromatography of albumins. It has also been used as a resin for purification of 3,4-dihydroxyphenylacetaldehyde (DOPAL)-bound α-synuclein (α-syn).

Physical form

Suspension in 0.5 M NaCl, 0.1 M sodium acetate, pH 5.0.

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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N Plotegher et al.
Scientific reports, 7, 40699-40699 (2017-01-14)
Parkinson's disease is a neurodegenerative disorder characterized by the death of dopaminergic neurons and by accumulation of alpha-synuclein (aS) aggregates in the surviving neurons. The dopamine catabolite 3,4-dihydroxyphenylacetaldehyde (DOPAL) is a highly reactive and toxic molecule that leads to aS
Francesco Longo et al.
Acta neuropathologica communications, 5(1), 22-22 (2017-03-16)
Mutations in the leucine-rich repeat kinase 2 (LRRK2) gene are the most common genetic cause of Parkinson's disease. Here, we investigated whether the G2019S LRRK2 mutation causes morphological and/or functional changes at nigro-striatal dopamine neurons. Density of striatal dopaminergic terminals
Orazio Angelo Arcidiacono et al.
International journal of molecular sciences, 21(21) (2020-11-05)
It has become evident that epitranscriptome events, mediated by specific enzymes, regulate gene expression and, subsequently, cell differentiation processes. We show that methyltransferase-like proteins METTL3/METTL14 and N6-adenosine methylation (m6A) in RNAs are homogeneously distributed in embryonic hearts, and histone deacetylase

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