A8530
m-Aminophenylboronic acid–Agarose
saline suspension
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About This Item
Numéro MDL:
Code UNSPSC :
12161501
ID de substance PubChem :
Nomenclature NACRES :
NA.32
Produits recommandés
Forme
saline suspension
Niveau de qualité
Ampleur du marquage
5-20 μmol per mL
Matrice
cross-linked 6% beaded agarose
Activation de la matrice
epoxy
Fixation de matrice
amino
Espaceur de matrice
12 atoms
Température de stockage
2-8°C
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Description générale
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).
Forme physique
Suspension in 0.5 M NaCl, 0.1 M sodium acetate, pH 5.0.
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°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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