Glycobiology
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).
Product information
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.
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