從醣蛋白中切除完整的醣鏈，高穩定性酵素製作過程不含甘油、氯化鈉，或其他添加物 所有的酵素經過測試不含蛋白水解活性及非預期的醣苷活性
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| 產品貨號 | 產品名稱 | 產品描述 | 產品規格 (Datasheet) |
|---|---|---|---|
| E-PNG01-20 | PNGase F – 0.1U/20ul | QA-Bio™ PNGase F cleaves asparagine-linked (N-linked) oligosaccharides from glycoproteins. PNGase F deaminates asparagine to aspartic acid, leaving the oligosaccharides intact. Denaturation increases the rate of cleavage up to 100x. Most native proteins can still be completely N-deglycosylated but incubation time must be increased. PNGase F will remain active under incubation conditions for at least 72 hours. PNGase F will not remove oligosaccharides containing Alpha-(1,3)-linked core fucose commonly found on plant glycoproteins; for this purpose, use peptide N-glycosidase A. | |
| E-PNG01 | PNGase F – 0.3U/60ul | QA-Bio™ PNGase F cleaves asparagine-linked (N-linked) oligosaccharides from glycoproteins. PNGase F deaminates asparagine to aspartic acid, leaving the oligosaccharides intact. Denaturation increases the rate of cleavage up to 100x. Most native proteins can still be completely N-deglycosylated but incubation time must be increased. PNGase F will remain active under incubation conditions for at least 72 hours. PNGase F will not remove oligosaccharides containing Alpha-(1,3)-linked core fucose commonly found on plant glycoproteins; for this purpose, use peptide N-glycosidase A. | |
| E-PNG05 | PNGase F – 1U/200ul | QA-Bio™ PNGase F cleaves asparagine-linked (N-linked) oligosaccharides from glycoproteins. PNGase F deaminates asparagine to aspartic acid, leaving the oligosaccharides intact. Denaturation increases the rate of cleavage up to 100x. Most native proteins can still be completely N-deglycosylated but incubation time must be increased. PNGase F will remain active under incubation conditions for at least 72 hours. PNGase F will not remove oligosaccharides containing Alpha-(1,3)-linked core fucose commonly found on plant glycoproteins; for this purpose, use endoglycosidase A. | |
| E-EF01 | Endoglycosidase F1, 1U/60ul | QA-Bio™ Endo F1 cleaves Asparagine-linked high mannose or hybrid oligosaccharides. It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide, generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. In contrast, PNGase F removes the oligosaccharide intact. | |
| E-EF02 | Endoglycosidase F2, 0.3U/60ul | QA-Bio™ Endo F2 cleaves Asparagine-linked high mannose or biantennary oligosaccharides. It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide, generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. In contrast, PNGase F removes the oligosaccharide intact. | |
| E-EF03 | Endoglycosidase F3, 0.3U/60ul | QA-Bio™ Endo F3 cleaves free or Asparagine-linked triantennary or fucosylated biantennary oligosaccharides,as well as triamnnosyl chitobiose core structures. It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide, generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. In contrast, PNGase F removes the oligosaccharide intact. Alpha 1-3 fucosylation will inhibit enzymatc activity. The recombinant version is not glycosylated, which may result in properties differing from the native protein. | |
| E-EH02 | Endo H (Endoglycosidase H), 300mU/60ul | QA-Bio™ Endo H cleaves Asparagine-linked hybrid or high mannose oligosaccharides, but not complex oligosaccharides. It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide, generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. In contrast, PNGase F removes the oligosaccharide intact. Detergent and heat denaturation may increase the rate of cleavage for some glycoproteins. | |
| E-G001 | O-Glycosidase, 75mU/60ul | Cleaves only unsubstituted Gal-ß(1-3)GalNAcalpha disaccharides attached to the serine or threonine residues of glycoproteins or glycopeptides. Substitutions such as sialic acid, galactose, fucose or N-acetylglucosamine must first be removed with the appropriate exoglycosidase prior to treatment with O-Glycosidase. At minimum, a sialadase such as Sialidase Au (Alpha-2-3,6,8,9), part number E-S001, is almost always required to remove sialic acids. |
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