| Description | Microbial derived chondroitin sulfate (CS)/dermatan sulfate (DS) sugar chain degrading enzymes (CSases) belong to polysaccharide lyases, which break the β -1,4-glycosidic bond between N-acetylglucosamine (GalNAc) and hexuronic acid (GlcUA/IdoUA) through a b-elimination reaction. At the same Microbial derived chondroitin sulfate (CS)/dermatan sulfate (DS) sugar chain degrading enzymes (CSases) belong to polysaccharide lyases, which break the β -1,4-glycosidic bond between N-acetylglucosamine (GalNAc) and hexuronic acid (GlcUA/IdoUA) through a b-elimination reaction. At the same time, unsaturated double bonds are formed between the C4 and C5 carbon atoms of the uronic acid, which have characteristic absorption at 232 nm and can be conveniently used for oligosaccharide product analysis and detection. Commercialized CSases include CSase ABC from Proteus vulgaris, which can simultaneously degrade CS, DS, and HA. In fact, CSase ABC is a mixture of two enzymes, with CSase ABCI being a CS/DS endonuclease and CSase ABCII being a non reducing end exonuclease of CS/DS; CSase ACI and B from Flavobacterium heparinum, where CSase ACI is a CS and HA specific endonuclease, while the latter is a DS specific endonuclease; The CSase ACII from Arthrobacter auricens is another CS and HA specific degrading enzyme, but it is an exonuclease that can effectively cleave the enzyme labeled with tetrasaccharides at the reducing end of CS oligosaccharides after being fluorescently labeled. Therefore, it is particularly useful in CS oligosaccharides enzymatic sequencing. CS/DS lyase is not only an important tool enzyme for studying the structure-activity relationship of CS/DS and preparing CS/DS oligosaccharides, but also has significant clinical application value in the treatment of central nervous system injuries. We can provide customers with various CSases with different substrate selectivity, substrate degradation modes, and specifications according to their needs, meeting various needs such as CS/DS structural and functional analysis, product quality testing, heparin/heparan sulfate production and purification, and large-scale enzymatic hydrolysis preparation of CS and DS functional oligosaccharides... Read More | Inquire | Product DescriptionEndo F1 cleaves Asparagine-linked high mannose and some hybrid oligosaccharides. Core fucosylation reduces the activity by 50 fold. Endoglycosidase F1 will hydrolyze sulfate containing high-mannose chains. It cleaves between the two N-acetylglucosamine residues in the Product DescriptionEndo F1 cleaves Asparagine-linked high mannose and some hybrid oligosaccharides. Core fucosylation reduces the activity by 50 fold. Endoglycosidase F1 will hydrolyze sulfate containing high-mannose chains. 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.Molecular weight 32,000 daltonsContents60 µl aliquot of enzyme (1 U) in 20 mM Tris-HCl, pH 7.5Included with 20 µL and 60 µL pack sizes:5x Reaction Buffer – 250 mM sodium phosphate, pH 5.5Specific ActivityDefined as the amount of enzyme required to catalyze the release of N-linked oligosaccharides from 1 micromole of denatured Ribonuclease B (RNase B) in 1 minute at 37°C, pH 5.5. Cleavage is monitored by SDS-PAGE (cleaved RNase B migrates faster).FormulationThe enzyme is provided as a sterile-filtered solution in 20 mM Tris-HCl, pH 7.5StabilitySeveral days exposure to ambient temperatures will not reduce activity. Stable at least 12 months when stored properly. SpecificityEndo 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. Quality & PurityEndo F1 is tested for contaminating protease as follows: 10 µg of denatured BSA is incubated at 37°C for 24 hours with 2 µl of enzyme. SDS-PAGE analysis of the treated BSA shows no evidence of degradation. The production host strain has been extensively tested and does not produce any detectable glycosidases.Directions for use1. Add up to 200 µg of glycoprotein to an Eppendorf tube. Adjust to 38 µl final volume with de-ionized water.2. Add 10 µl 5x Reaction Buffer 5.53. Add 2.0 µl of Endo F1 to the reaction. Incubate 1 hour or more at 37°C.Monitor cleavage by SDS-PAGE... Read More | The Leuconostoc GPDH exhibits dual coenzyme specificity, namely NAD and NADP (Olive and Levy, Biochem., 6, 730 730, 1967). When assayed under conditions that are optimal for the particular coenzyme, the ratio of observed catalytic activity is NAD/NADP = 1.8 | Inquire |