Glyko® 2-AA-(Human α 1-acid glycoprotein N-Linked Glycan Library) 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; constituting a heterogenous mixture of core non-fucosylated bi-, tri- and tetraantennary glycans with various degree of sialylation (NeuAc) and some with outer arm fucose residues and lactosamine repeats, consistent with N-glycans reviously 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 also may be substituted with fucose which results in formation of sialyl Lewis X-like structure.
The sialic acid residues are found both in α(2-3) and α(2-6) linkages. The composition of the library is approximately as follows: monosialylated glycans ~1%, di-sialylated ~20%, tri-sialylated ~51% and tetrasialylated ~27%. Triantennary glycans are a major component and constitute ~44% of total glycans present in the Human "1-acid Glycoprotein N-linked Glycan Library. The reducing termini are derivatized with the fluorescent dye, 2-AA.
Please contact us for a representative Certificate of Analysis.
Size: 200 pmol
Product Code: GKSA-001
Product Safety Documentation for GKSA-001:
|GKSA-001||Glyko® 2-AA Human α1-Acid Glycoprotein N-Linked Glycan Library|||
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