Glycan analysis often involves structural determination of oligosaccharide components of glycoproteins, glycolipids, glycosphingolipids, and other glycan-containing biological molecules.
Sensitive carbohydrate chemistry techniques require specific enzymes such as fucosidase, sialidase, biosidase, and other hydrolytic enzymes with activities specific for certain linkages. Sequential treatment of glycan-containing samples can allow structural determination of the original moiety, a fundamental technique of glycan analysis.
Precise, pure enzymes from Takara Bio for carbohydrate chemistry analyses include alpha-1,2 fucosidase, alpha-1,3/1,4 fucosidase, alpha 2,3-sialidase, Lacto-N-biosidase, and glycan hydrolases useful for sphingolipid analysis such as recombinant endoglycoceramidase II.
In some situations such as proteomic analysis, it may be desirable to remove oligosaccharide structures prior to analysis of protein fractions by MALDI-TOF mass spectrometry. PNGase (also known as glycopeptidase F) is widely used for this purpose to deglycosylate protein samples.
Additional products for glycoprotein research include the Sialic Acid Florescence Labeling Kit for efficient modification of sialic acid-containing moieties with DMB prior to detection by HPLC, and kits for purification of glycan samples (including hydrazine-treated samples) prior to fluorescent labeling with 2-aminopyridine (pyridylamination reaction).
Fast, simple, and efficient protein digestion with Capturem Trypsin
Capturem Trypsin digests proteins more rapidly and completely than trypsin in solution, as demonstrated using apomyoglobin, a common protein mapping standard, and myoglobin, a tightly folded protein. This makes it a powerful tool for proteomic analysis. Apomyoglobin peptides generated by Capturem Trypsin digestion were shown to provide good sequence coverage using mass spectrometry, while digestion of a whole-cell lysate enabled the identification of 2,320 unique proteins via LC/MS-MS analysis.
