QA-Bio Endoglycosidases 醣苷內切酶

Endoglycosidases 醣苷內切酶 ,是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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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

產品貨號產品名稱產品描述產品規格(Datasheet)
E-PNG01-20PNGase F – 0.1U/20ulQA-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.PDF
E-PNG01PNGase F – 0.3U/60ulQA-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.PDF
E-PNG05PNGase F – 1U/200ulQA-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.PDF
E-EF01Endoglycosidase F1, 1U/60ulQA-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.PDF
E-EF02Endoglycosidase F2, 0.3U/60ulQA-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.PDF
E-EF03Endoglycosidase F3, 0.3U/60ulQA-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.PDF
E-EH02Endo H (Endoglycosidase H), 300mU/60ulQA-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.PDF
E-G001O-Glycosidase, 75mU/60ulCleaves 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.PDF
E-XBG01Endo-Beta-Galactosidase, 0.9U/60ulEndo-β-Galactoctosidase (EC 3.2.1.103) cleaves internal β(1- 4) galactose linkages in unbranched, repeating poly-Nacetyllactosamine structures. Sulfated structures such as keratan sulfate are also cleaved. Branching and/or fucosylation of the substrate may decrease or eliminate cleavage. Endo-β-Galactoctosidase is useful for identifying and removing poly-N-acetyllactosamine structures on many biologically important glycoconjugates.PDF