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A8312

Sigma-Aldrich

m-Aminophenylboronic acid–Agarose

aqueous suspension

Synonym(s):

(3-aminophenyl)boronic acid-Agarose, 3-Aminophenylboronic acid–Agarose, m-APBA-Agarose, m-Aminophenylboronic acid resin

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About This Item

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

form

aqueous suspension

extent of labeling

40-80 μmol per mL

matrix

6% beaded agarose

matrix activation

epichlorohydrin

matrix attachment

through amino to carboxyls of EDTA

matrix spacer

9 atoms

capacity

≥8 mg/mL binding capacity (peroxidase Type VI)

storage temp.

2-8°C

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General description

m-Aminophenylboronic acid (m-APBA) immobilized on an agarose gel is useful in immunoglobulins capture, but also leads to non-specific interactions. m-APBA is a boronate affinity matrix that is effectively used for affinity purification of monoclonal antibodies.

Application

m-Aminophenylboronic acid-Agarose has been used:
  • as a component of the column for the purification of Escherichia coli TOP10F cells
  • with cell lysates of various cells for detection of PARylated (Poly(ADP-ribos)ylation) proteins.
  • in the affinity purification of horseradish peroxidase (HRPO)
  • in the glycated human serum albumin (gHSA) purification

Physical form

Suspension in water containing 0.002% chlorhexidine diacetate.

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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T A Myöhänen et al.
The Biochemical journal, 197(3), 683-688 (1981-09-01)
The synthesis of 3-nitro-4-(6-aminohexylamido)phenylboronic acid is described. The properties of two novel forms of immobilized phenylboronate agarose adsorbents [m-aminophenylboronic acid-Matrex Gel and 3-nitro-4-(6-aminohexylamido)phenylboronic acid-Sepharose CL-6B] were investigated. Both gels bind and selectively retard the glycoprotein alpha-glucosidase from yeast. The retardation
Monika Kijewska et al.
Molecules (Basel, Switzerland), 25(3) (2020-02-14)
We report herein a novel ChemMatrix® Rink resin functionalised with two phenylboronate (PhB) moieties linked on the N-α and N-ε amino functions of a lysine residue to specifically capture deoxyfructosylated peptides, compared to differently glycosylated peptides in complex mixtures. The
RUNX poly (ADP-ribosyl) ation and BLM interaction facilitate the Fanconi anemia pathway of DNA repair
Tay L S, et al.
Testing, 24(7), 1747-1755 (2018)
Construction and optimization of a CC49-Based scFv-beta-lactamase fusion protein for ADEPT
Roberge M, et al.
Protein engineering, design & selection : PEDS, 19(4), 141-145 (2006)
Qian Chen et al.
The EMBO journal, 40(2), e104542-e104542 (2020-12-03)
Optimal DNA damage response is associated with ADP-ribosylation of histones. However, the underlying molecular mechanism of DNA damage-induced histone ADP-ribosylation remains elusive. Herein, using unbiased mass spectrometry, we identify that glutamate residue 141 (E141) of variant histone H2AX is ADP-ribosylated

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