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GlycoProfile™ 2-AB Labeling Kit

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NACRES:
NA.32

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General description

The GlycoProfile™ labeling kits are designed for efficient labeling of N-linked, O-linked, and glycosyl­phosphatidyl­inositol (GPI) anchored glycans with either 2-aminobenzamide (2-AB) or 2-aminobenzoic acid (anthranilic acid; 2-AA). These small fluorophores increase the spectral absorption of glycans, improving the detection of labeled glycans by HPAE (high-performance anion exchange chromatography), HPLC, and ESI-MS (electrospray mass spectroscopy) methods. Binding is robust and the resulting dye-glycan conjugates are stable, with no degradation during post-labeling analysis.

Application

GlycoProfile™ 2-AB Labeling Kit has been used for the labelling of N-linked glycans from human IgG, Bovine fetuin, and human epididymis protein 4. It has also been used for labelling free oligosaccharides from mouse spleen.
While 2-AB is slightly less sensitive than 2-AA, it is suitable for downstream glycan analysis by HPAE, HPLC and ESI-MS. Although suitable for the same applications, 2-AA is better suited for SDS-PAGE.

Legal Information

Labeling of glycans with 2-AB is covered under US Patent No. 5,747,347 and its foreign equivalents.
GlycoProfile is a trademark of Sigma-Aldrich Co. LLC

Kit Components Only

Product No.
Description
  • 2-AB Labeling Reagent 2 x 5
  • Dimethyl sulfoxide (DMSO) 2 x 350
  • Acetic acid, glacial 2 x 200
  • Reductant (sodium cyanoborohydride) 2 x 6

Signal Word

Danger

Hazard Classifications

Acute Tox. 2 Dermal - Acute Tox. 2 Inhalation - Acute Tox. 2 Oral - Aquatic Acute 1 - Aquatic Chronic 1 - Eye Dam. 1 - Flam. Sol. 1 - Skin Corr. 1A - Water-react 1

Supplementary Hazards

EUH032

Storage Class Code

4.3 - Hazardous materials, which set free flammable gases upon contact with water

WGK

WGK 3

Regulatory Information

危险化学品

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Separation of 2-aminobenzamide labeled glycans using hydrophilic interaction chromatography columns packed with 1.7 mum sorbent
Ahn J, et al.
Journal of Chromatography. B, Biomedical Sciences and Applications, 878(3-4), 403-408 (2010)
Expression and biochemical characterization of recombinant human epididymis protein 4
Hua L, et al.
Protein Expression and Purification, 102, 52-62 (2014)
Florian Cambay et al.
Current research in immunology, 1, 23-37 (2020-06-27)
The effector functions of the IgGs are modulated by the N-glycosylation of their Fc region. Particularly, the absence of core fucosylation is known to increase the affinity of IgG1s for the Fcγ receptor IIIa expressed by immune cells, in turn
Enhancing the antiviral potency of ER alpha-glucosidase inhibitor IHVR-19029 against hemorrhagic fever viruses in vitro and in vivo
Ma J, et al.
Antiviral research, 150, 112-122 (2018)
Belinda L Spillings et al.
Cell reports, 38(5), 110296-110296 (2022-02-03)
Here, we present ultrastructural analyses showing that incoming HIV are captured near the lymphocyte surface in a virion-glycan-dependent manner. Biophysical analyses show that removal of either virion- or cell-associated N-glycans impairs virus-cell binding, and a similar glycan-dependent relationship is observed
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Glycan Labeling

Structural modifications of proteins are essential to living cells. When aberrantly regulated they are often the basis of disease. Glycans are responsible for much of the structural variation in biologic systems, and their representation on cell surfaces is commonly called the “glycome.”

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