Prozyme 代理

Glyko® PNGase F (Chryseobacterium [Flavobacterium] meningosepticum)

Specificity:

PNGase F releases intact N-linked oligosaccharides from glycoproteins and glycopeptides. The enzyme will not cleave oligosaccharides from a single asparagine residue and cleavage does not occur if there is core α1-3 linked fucose as commonly encountered in plant glycoproteins Phosphate, sulfate and sialic acid groups attached to the oligosaccharide do not affect cleavage.

Applications:

• release of intact N-linked glycans from glycopeptides and glycoproteins
• structure-function studies of N-glycosylated glycoproteins
• preparation of deglycosylated proteins for molecular weight estimation or crystallography studies

Glyko® N-Glycanase (recomb Chryseobacterium [Flavobacterium] meningosepticum, expressed in E. coli)

Recombinant PNGase F is covered by US Patent No 5,238,821 and EP Patent No 0472651 B1, exclusively licensed for manufacture by ProZyme®, Inc.

Purchase includes a limited license to use.

[Peptide-N-glycosidase F, PNGase F] cleaves all asparagine-linked complex, hybrid or high mannose oligosaccharides unless α(1-3) core fucosylated; asparagine must be peptide-bonded at both termini. Phosphate, sulfate and sialic acid groups attached to the oligosaccharide do not affect cleavage. Endo F free.

"A & B" pack size ships with WS0010 5x N-Glycanase® Reaction Buffer,

WS0012 Denaturation Solution & WS0013 Detergent Solution

Highly concentrated, particularly useful for deglycosylation under native conditions.

Not formulated for FACE® Analysis, use GK50052 instead

Glyko® N-Glycanase (recomb Chryseobacterium [Flavobacterium] meningosepticum, expressed in E. coli)

Recombinant PNGase F is covered by US Patent No 5,238,821 and EP Patent No 0472651 B1, exclusively licensed for manufacture by ProZyme®, Inc.

Purchase includes a limited license to use.

[Peptide-N-glycosidase F, PNGase F] cleaves all asparagine-linked complex, hybrid or high mannose oligosaccharides unless α(1-3) core fucosylated; asparagine must be peptide-bonded at both termini. Phosphate, sulfate and sialic acid groups attached to the oligosaccharide do not affect cleavage. Endo F free.

"A & B" pack size ships with:

WS0010 - 5x N-Glycanase® Reaction Buffer

WS0012 - Denaturation Solution

WS0013 - Detergent Solution

Highly concentrated, particularly useful for deglycosylation under native conditions.

Not formulated for FACE® Analysis, use GK50052 instead

Glyko® N-Glycanase (recomb Chryseobacterium [Flavobacterium] meningosepticum, expressed in E. coli)

Recombinant PNGase F is covered by US Patent No 5,238,821 and EP Patent No 0472651 B1, exclusively licensed for manufacture by ProZyme®, Inc.

Purchase includes a limited license to use.

[Peptide-N-glycosidase F, PNGase F] cleaves all asparagine-linked complex, hybrid or high mannose oligosaccharides unless α(1-3) core fucosylated; asparagine must be peptide-bonded at both termini. Phosphate, sulfate and sialic acid groups attached to the oligosaccharide do not affect cleavage. Endo F free.

"A & B" pack size ships with WS0010 5x N-Glycanase® Reaction Buffer,

WS0012 Denaturation Solution & WS0013 Detergent Solution

Highly concentrated, particularly useful for deglycosylation under native conditions.

Not formulated for FACE® Analysis, use GK50052 instead

Glyko® N-Glycanase-PLUS (recomb Chryseobacterium [Flavobacterium] meningosepticum, in E. coli)

• Glycanase is widely used for the removal of N-glycans from glycoproteins and glycopeptides. It is well known that denaturation of glycoprotein substrates before enzyme digestion dramatically increases the efficiency of their deglycosylation,

allowing complete removal of most classes of N-glycans from glycoproteins. NOTE: The source organism was previously known as Chryseobacterium [Flavobacterium] meningosepticum Peptide-N-glycosidase F, PNGase F] cleaves all asparagine-linked complex, hybrid or high mannose oligosaccharides unless α(1-3) core fucosylated; asparagine must be peptide-bonded at both termini. Phosphate, sulfate and sialic acid groups attached to the oligosaccharide do not affect cleavage. Endo F free.

"B" pack size ships with WS0010 5x N-Glycanase Reaction Buffer,

WS0012 Denaturation Solution & WS0013 Detergent Solution

Highly concentrated, particularly useful for deglycosylation under native conditions.

Not formulated for FACE® Analysis, use GK50052 instead

Recombinant PNGase F is covered by US Patent No 5,238,821 and EP Patent No 0472651 B1, exclusively licensed for manufacture by ProZyme®, Inc.

Purchase includes a limited license to use.

Glyko® N-Glycanase-PLUS (recomb Chryseobacterium [Flavobacterium] meningosepticum, in E. coli)

• Glycanase is widely used for the removal of N-glycans from glycoproteins and glycopeptides. It is well known that denaturation of glycoprotein substrates before enzyme digestion dramatically increases the efficiency of their deglycosylation,

allowing complete removal of most classes of N-glycans from glycoproteins. NOTE: The source organism was previously known as Chryseobacterium [Flavobacterium] meningosepticum Peptide-N-glycosidase F, PNGase F] cleaves all asparagine-linked complex, hybrid or high mannose oligosaccharides unless α(1-3) core fucosylated; asparagine must be peptide-bonded at both termini. Phosphate, sulfate and sialic acid groups attached to the oligosaccharide do not affect cleavage. Endo F free.

"B" pack size ships with WS0010 5x N-Glycanase Reaction Buffer,

WS0012 Denaturation Solution & WS0013 Detergent Solution

Highly concentrated, particularly useful for deglycosylation under native conditions.

Not formulated for FACE® Analysis, use GK50052 instead

Recombinant PNGase F is covered by US Patent No 5,238,821 and EP Patent No 0472651 B1, exclusively licensed for manufacture by ProZyme®, Inc.

Purchase includes a limited license to use.

Glyko® Endoglycosidase H (recombinant gene from Streptomyces plicatus, expressed in E. coli)

The enzyme cleaves between the N-acetylglucosamine residues of the chitobiose core of N-linked glycans. The enzyme will cleave oligomannose and most hybrid type glycans, including those which are core fucosylated, whereas complex type glycans are not hydrolyzed

Glyko® Endoglycosidase F2 (recombinant gene from Chryseobacterium [Flavobacterium] meningosepticum expressed in E. coli) The enzyme cleaves within the di-N-acetyl chitobiose core of high mannose and biantennary complex type asparagine linked glycans of oligosaccharide, glycopeptide or glycoprotein substrates. It hydrolyzes biantennary glycans at a rate approximately 20 times higher than high mannose glycans. The enzyme is not active towards hybrid type or tri- and tetraantennary oligosaccharides.

Applications:

• Selective release of high mannose and biantennary complex type asparagine linked oligosaccharides from glycopeptides/ glycoproteins.

   

   

Glyko® O-Glycanase (recombinant gene from Streptococcus pneumoniae, expressed in E.coli)

[Endo-O-Glycosidase™, Endo-α-N-acetylgalactosaminidase, O-Glycosidase] releases unsubstituted, Ser/Thr-linked GalGalNAc from proteins; used with additional enzymes to remove more complex O-linked structures.

Exoglycosidases

Glyko® Sialidase S™/NANase I (recombinant from Streptococcus pneumoniae, expressed in E. coli) [neuraminidase] release sialic acid from complex carbohydrates.

Glyko® Sialidase C™/NANase II (recombinant from Clostridium perfringens, expressed in E. coli)

[neuraminidase], releases α(2-3,6)-linked sialic acid from complex carbohydrates

Glyko® Sialidase A™/NANase III (recombinant gene from Arthrobacter ureafaciens, expressed in E. coli)

Specificity:

The enzyme releases α2-3, α2-6, α2-8, and α2-9 linked N-acetylneuraminic acid from complex carbohydrates. The initial rate of hydrolysis of α2-6 linkages is reported to be approximately twice that of α2-3 linked sialic acid however, in practice, this kinetic selectivity is of little consequence during extended incubations. Effective digestion of glycolipid substrates is facilitated by addition of a detergent, such as sodium taurodeoxycholate to the incubation.

Glyko® Sialidase A™ Sampler Kit

This Sampler Kit contains 1 vial each of 3 isoforms (88, 66 and 51 kDa) of the enzyme Sialidase A™™ (recombinant gene from Arthrobacter ureafaciens expressed in E. coli).

Each enzyme vial contains 200 mU in 40 µl. Also included is one vial 5x Reaction Buffer (1 ml). These products are available for purchase separately in 1-Unit pack sizes under the individual product codes.

Glyko® Sialidase A™-66 (recombinant gene from Arthrobacter ureafaciens, expressed in E. coli)

Glyko® Sialidase A™-66 (recombinant gene from Arthrobacter ureafaciens, expressed in E. coli) MW - 66 kDa

Glyko® Sialidase N™ (Newcastle disease virus, Hitchner B1 Strain)

Specificity:

This sialidase is highly α2-3 linkage specific, cleaving non-reducing terminal sialic (N-acetyl neuraminic, NeuNAc) acid α2-3 linked to galactose or N-acetylgalactosamine. It also cleaves α2-8 linked sialic acid, commonly encountered in polysialic acid. Cleavage of sialic acid α2-6 linked to galactose, N-acetyl-galactosamine or N-acetylglucosamine does not occur. There is some specificity towards the N- and O- acylation patterns of the sialic acids.

Applications:

• This sialidase is the most highly selective commercially available enzyme for removal of α2-3 linked sialic acid and as such has been extensively used for the removal of sialic acid and, in conjunction with broader specificity sialidases for the analysis of sialylation patterns of both lipid and protein associated glycoconjugates in isolated and whole cell systems.

   

   

Glyko® Sialidase T™ (recombinant gene from Salmonella typhimurium, expressed in E. coli)

Specificity:

This sialidase has a 260-fold kinetic preference for α2-3 linked over α2-6 linked terminal sialic acid. This bias is not unusual for bacterial sialidases, but the magnitude is somewhat greater than others. This preference puts the enzyme from S. typhimurium between that from Newcastle disease virus (Cat No: X-5017) which is effectively α2-3 specific and from C. perfringens (Cat No: X-5020) which show approximately 3-fold preference for this linkage.

Despite the preference for α2-3 linked sialic acid the S. typhimurium enzyme is also active against α2-6 linked sialic acid and when the enzyme is used in excess, these linkages can be completely degraded.

Applications:

• This sialidase's activity at physiological pH and ionic strengths make it an ideal candidate for the modification of intact cells as well as isolated glycoconjugates. The ability to digest gangliosides efficiently, even in the absence of detergent confirms this.

   

   

Glyko® Sialidase V™ (Vibrio cholerae)

Supplied as 1U (200µl) [Neuraminidase], α(2-3,6,8)-specific, releases sialic acid from oligosaccharides. A sterile-filtered solution in 50 mM sodium acetate, 154

CaCl2, 0.1% (w/v) Micr-O-protect, 10 mM EDTA and ~100 :g/ml HSA4

(pH 5.5)mM NaCl, 9 mM

Glyko® Sialidase I (recombinant gene from Clostridium perfringens, expressed in E. coli)

Specificity:

This enzyme has a broad specificity, active against isolated oligosaccharides, gangliosides, glycoproteins and mucins. The enzyme favors cleavage of α2,3 linked N-acetylneuraminic acid by a factor of about 2.5-3.0, but in practice distinction between these linkages in practice does not occur. N-glycolyl derivatives of sialic acid are also cleaved efficiently.

O-acetylation can affect specificity. 9-O-acetyl neuraminic acid is cleaved, but, in contrast to Newcastle disease virus sialidase (Cat. No. X-5017), the 4-O-acetyl analogue is not cleaved. The enzyme will cleave gangliosides; this activity is enhanced by the presence of detergent, (although the enzyme from A.ureafaciens Cat.No. 80040) is more efficient in this application.

Applications:

The enzyme is an established tool for glycoconjugate research. It has been used in the structural and functional analysis of the role of sialic acids on all types of glycoconjugate, ranging from whole organs to isolated molecules; in all aspects of sialic acid biology, from viral and neurotransmitter receptor function to cancer diagnosis.

Glyko® β(1,3,6)-Galactosidase/GALase II (recomb from Xanthomonas manihotis, expressed in E. coli)

Releases non-reducing terminal β(1-3,6)-linked galactose from complex carbohydrates.

Ships with Incubation Buffer.

Glyko® β(1-4,6)-Galactosidase (jack bean)

The enzyme readily hydrolyses non-reducing terminal Galβ(1-6)GlcNAc and Galβ(1-4)GlcNAc. Galβ(1-3)GlcNAc is hydrolyzed very slowly. The relative rates of hydrolysis are: β(1-6), 100%; β(1-4) 75%; and β(1-3), 1%. Galβ(1-6) and Galβ(1-3) can also be released from other aglycones although the rates of hydrolysis are variable.

Glyko® β(1-3,4)-Galactosidase (bovine testis)Releases non-reducing terminal β(1-3,4)-linked galactose from oligosaccharides.

Glyko® β(1-4)-Galactosidase (Streptococcus pneumoniae)

Releases non-reducing terminal β(1-4)-linked galactose from oligosaccharides.

Glyko® β-N-Acetylhexosaminidase (jack bean)/HEXase III

Releases non-reducing terminal β(1-2,3,4,6)-linked N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) residues.

Glyko® β-N-Acetylhexosaminidase/HEXase I (recomb from Streptococcus pneumoniae, expressed in E. coli)

[N-acetyl-β-D-glucosaminidase], β(1-2,3,4,6)-specific, cleaves all non-reducing terminal β-linked N-acetylglucosamine; no activity on N-acetylgalactosamine. Use with GKX-5003 to determine the linkage position of β GlcNAc residues.

Glyko® α-N-Acetylgalactosaminidase (chicken liver)highly specific, cleaves terminal α(1-3)-linked N-acetylgalactosamine. Also cleaves GalNAc-Ser/Thr.

Glyko® α-Mannosidase/MANase VI (recombinant gene from Xanthomonas manihotis, expressed in E. coli)

Releases non-reducing terminal unbranched α(1-6)-linked mannose attached to a β-mannose.

Glyko® α(1-3,4,6)-Galactosidase (green coffee bean)

Releases non-reducing terminal α(1-3,4,6)-linked galactose from oligosaccharides.

NOTE: Highly purified; β-galactosidase contaminating activity not detectable (extended incubation with 2-AB NA2)

Glyko® α(1-2)-Mannosidase (Aspergillus saitoi)

Releases non-reducing terminal α(1-2)-linked mannose from oligosaccharides.

NOTE: 2 mU is equal to 50µU as previously reported by Glyko®, Inc.

Glyko® α(1-2,3,6)-Mannosidase (jack bean)

Releases non-reducing terminal α(1-2,6,3)-linked mannose from oligosaccharides.

Glyko® β-Mannosidase (Helix pomatia)

Releases non-reducing terminal β(1-4)-linked mannose from oligosaccharides.

Glyko® α(1-2)Fucosidase/FUCase II (Xanthomonas manihotis)

Releases non-reducing terminal unbranched α(1-2)-linked fucose from complex carbohydrates.

Glyko® α(1-2,3,4,6)Fucosidase (bovine kidney)

Broad specificity; releases non-reducing terminal α(1-6) core-linked fucose more efficiently than other α-fucose linkages.

Glyko® α(1-3,4)-Fucosidase (almond meal)

The enzyme specifically cleaves non-reducing terminal α1-3 or α1-4 fucose residues.

After digestion with 0.2 mU/ml enzyme at a substrate concentration of 40 µM in 50 mM sodium acetate pH 5.0, 2 nmol of LNFPII is completely de-fucosylated. 3'fucosyllactose (2 nmol) was 65% de-fucosylated by 5 mU of a1-3/4 fucosidase during a 24hr incubation. However, under equivalent conditions, no fucose was release from 3' sialo-3-fucosyllactose. Higher enzyme concentrations (>2 mU/ml) are found to be required for the removal of α1-3 or α1-4 fucose residues from complex N-glycans. Complete hydrolysis of Fuc α1-3 GlcNAc from the outer arms of a di α1-3 fucosylated, di α1-2 fucosylated bi-antennary N-glycan isolated from Human parotid gland was obtained at a final substrate concentration of 1 mM and a final enzyme concentration of 3 mU/ml.

Applications:

• The enzyme can be used in the analysis of fucosylated O- and N-linked glycans during exoglycosidase sequencing It has also been used in the analysis and modification of blood group oligosaccharides since it is active towards the Lex antigen.

GAG

Glyko® β-D-Glucuronidase (Bovine liver)