Product Description
AdvanceBio 2-AA Human α-1-acid glycoprotein N-glycan library (formerly ProZyme). Library is derived from α-1-acid glycoprotein, which is heavily glycosylated (~45% carbohydrates) and contains five N-glycosylation sites. The Human α1-Acid glycoprotein N-linked glycan library represents a total pool of N-linked glycans released from Human α1-acid glycoprotein. These glycans constitute a heterogenous mixture of core non-fucosylated bi-, tri- and tetraantennary glycans with various degrees of sialylation (NeuAc) and some with outer arm fucose residues and lactosamine repeats, consistent with N-glycans previously reported for human α1-acid glycoprotein. The biantennary glycans can have one or two sialic acid residues. The triantennary and tetraantennary glycans can have from one to four sialic acid residues and may be substituted with fucose, resulting in formation of sialyl Lewis X like structure.
Specifications:
Label: 2-AA
Unit: 200 pmol
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The AdvanceBio 2-AA Human alpha-1-acid glycoprotein N-glycan library offers a well-characterized set of N-glycans enzymatically released from purified human alpha-1-acid glycoprotein and labeled with 2-aminobenzoic acid 2-AA. This ready-to-use glycan library enables accurate identification, qualitative comparison, and method development for glycan analysis in biopharmaceutical research. Suitable for use as system suitability controls, retention time markers, and reference standards, it is ideal for HILIC and HPLC, as well as for CE and other fluorescence-based applications. Laboratories focused on glycoprotein characterization, biosimilar comparability, biomarker discovery, or academic glycomics studies can benefit from this library to enhance reproducibility and confidence in data interpretation. The library is fully compatible with Agilent AdvanceBio Glycan Mapping columns and Agilent HPLC or LC-MS systems, and may also be used with a variety of analytical platforms supporting fluorescently labeled glycan analysis. For streamlined workflows, integration with Agilent MassHunter or similar software supports efficient data processing. The trusted quality portfolio and consistent labeling support high-performance and reproducible results in comprehensive glycan structure assignment and profiling tasks in regulated and research environments.
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Collaboration
Tony Tang
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