| Description | Product DescriptionEndo-Beta-Galactosidase cleaves internal β(1-4) galactose linkages in unbranched, repeating poly-N-acetyllactosamine structures. Sulfated structures such as keratan sulfate are also cleaved. Branching and/or fucosylation of the substrate may decrease or eliminate cleavage.Product DescriptionEndo-Beta-Galactosidase cleaves internal β(1-4) galactose linkages in unbranched, repeating poly-N-acetyllactosamine structures. Sulfated structures such as keratan sulfate are also cleaved. Branching and/or fucosylation of the substrate may decrease or eliminate cleavage.Endo-Beta-Galactosidase is useful for identifying and removing poly-N-acetyllactosamine structures on many biologically important glycoconjugates.Contents60 µl aliquot of enzyme (0.9 U) in 20 mM tris-HCl, pH 7.51 vial reaction buffer- 250mM Sodium phosphate, pH 5.8pH Optimum: 5.8Molecular Weight32,000 daltonsFormulationThe enzyme is provided as a sterile-filtered solution in 20 mM Tris-HCl, pH 7.5StabilityStable at least 12 months when stored properly. Several days exposure to ambient temperatures will not reduce activity. Active at least 5 days under reaction conditions.SpecificityInternal β(1-4) galactose linkages in unbranched, repeating poly-N-acetyllactosamine [GlcNAcβ(1-3) Galβ(1-4)]n structures are the preferred substrate. Sulfated structures such as keratan sulfate are also cleaved. Branching and/or fucosylation of the substrate may decrease or eliminate cleavage. Sulfation of C-6 on galactose will block cleavage. Oligosaccharidesof the neo-lacto group are cleaved at greatly educed rates depending on the deviation from the preferred substrate.For example, Galβ(1-3)GlcNAcβ(1-3)Galβ(1-4)Glc is cleaved at 5x10-5 the rate of keratan sulfate(see ref.4). Specificity is similar to the Escherichia freundii enzyme. except that it is limited to cleaving N-acetyllactosamine extensions on tetraantennary structures of erythropoietin(see ref 5).Specific ActivityOne unit of endo-β-Galactosidase is defined as the amount that will liberate one µmole of reducing sugar per minute at 37℃and pH 5.8 from bovine corneal keratan sulfate. Purity Endo-β-Galactosidase is tested for contaminating protease as follows: 10 ug of denatured BSA is incubated for 24 hours at 37℃ with 2 µl of enzyme. SDS-PAGE analysis of the treated BSA shows no evidence of degradation. The production strain of E. coli has been extensively tested and does not produce any detectable glycosidases.Directions for useFor glycoproteins:1. Add up to 100 µg of glycoprotein to a tube.2. Add 4 ul 5X buffer and water to 19 µl.3. Add 1 µl enzyme.4. Incubate at 37℃ for 2 hrs.Procedure for oligosaccharides:Same as above except incubate from several hours to several days depending on the substrate. Add bovine serum albumen to 2 mg/ml to stabilize the protein during extended incubations.ApplicationsEndo-β-Galactosidase (EC 3.2.1.103) cleaves internal β(1-4) galactose linkages in unbranched, repeating polyN-acetyllactosamine structures. Sulfated structures such as keratan sulfate are also cleaved. Branching and/or fucosylation of the substrate may decrease or eliminate cleavage. Endo-β-Galactosidase is useful for identifying and removing poly-N-acetyllactosamine structures on many biologically important glycoconjugates... Read More | Product IntroduceProteinase K, originally isolated from the mold Tritirachium album, is a serine protease with broad substrate specificity and relatively high proteolytic activity. It preferentially cleaves ester and peptide bonds adjacent to the C-termini of hydrophobic, aliphatic, or aromatic Product IntroduceProteinase K, originally isolated from the mold Tritirachium album, is a serine protease with broad substrate specificity and relatively high proteolytic activity. It preferentially cleaves ester and peptide bonds adjacent to the C-termini of hydrophobic, aliphatic, or aromatic amino acids. aladdin's proteinase K is characterized by high purity, sterility, no bio-burden, and no presence of DNAse, RNAse, DNA, and RNA contaminants. It is a good partner in DNA and RNA extraction for you.Features1、According to the SDS-PAGE image,the purity of Proteinase K is more than 95% and the molecular weight is 28.9 kDa.2、Detect DNase residue by agarose gel electrophores.3、Detect Nucleic acid residue by agarose gel electrophores.4、Detect RNase residue by agarose gel electrophores.5、Using the absorbance A275 as the vertical axis and different concentrations of tyrosine as the horizontal axis, a standard curve was drawn, and the enzyme activity was calculated>30U/mg... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： Neuron specific enolase (NSE), also known as ENO2 or gamma-enolase, is a dimeric, Mg2+-dependent enzyme that catalyzes the dehydration of 2-phospho-D glycate (PGA) to phosphoenolpyruvate (PEP) in the Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： Neuron specific enolase (NSE), also known as ENO2 or gamma-enolase, is a dimeric, Mg2+-dependent enzyme that catalyzes the dehydration of 2-phospho-D glycate (PGA) to phosphoenolpyruvate (PEP) in the glycolytic pathway and catalyzes the reverse reaction in gluconeogenesis. There are three major isozymes of enolase expressed in selective vertebrate tissues from separate genes: alpha (ENO1), beta (ENO3), and gamma (ENO2). NSE is a highly expressed, specific neuron isozyme making it a useful marker for tumors derived from neuronal cells. Neuron-specific enolase is implicated as a diagnostic and prognostic marker in numerous diseases including early small cell lung cancer, prostate cancer, multiple myeloma, traumatic brain injury, acute spinal cord injury, acute ischemic stroke, and post-concussion symptoms. NSE expression and activity are increased in neuronal and glial activation and injury, risk factors implicated in neurodegenerative disease. Elevation of NSE promotes glycolysis, proliferation, activation and migration through its C-terminus to activate PI3K and MAPK signal transduction pathways while inhibition of enolase has been shown to attenuate inflammatory events. NSE can be regulated through cleavage of the C-termini by cathepsin X or inhibited directly by antibiotic SF2312. Inhibition has been proposed as a therapeutic strategy in cancer... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： 100B, previously called S100 beta, belongs to the S100 family within the EF-hand superfamily of Ca2+ binding proteins. S100 proteins contain two EF-hand motifs that differ in affinity, separated by a hingePurity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： 100B, previously called S100 beta, belongs to the S100 family within the EF-hand superfamily of Ca2+ binding proteins. S100 proteins contain two EF-hand motifs that differ in affinity, separated by a hinge region with a hydrophobic cleft that is exposed upon Ca2+ binding. S100B is a 91 amino acid (aa) protein, after removal of the initial methionine, and is found as homodimers of 10.4 kDa monomers. Human S100B shares 99%, 98%, 100%, 99% and 97% aa sequence identity with mouse, rat, rabbit, equine and bovine S100B, respectively. Within the S100 family, human S100B shows the highest aa identity (59%) with S100A1. S100B is expressed primarily by astrocytes and oligodendrocytes in the central nervous system, and by Schwann cells in the peripheral nervous system. Ca2+-bound S100B interacts in vitro with at least 20 cytoplasmic proteins, including several structural molecules such as tubulin and GFAP. It can inhibit the phosphorylation of these kinase substrates and others such as tau and neuromodulin. Astrocytes can secrete S100B, which then acts in a cytokine-like manner. Nanomolar concentrations of S100B are secreted constitutively, promote proliferation, and are neurotrophic and anti-apoptotic. Blood levels of S100B reflect extracellular concentrations within the nervous system, and are elevated in Down’s syndrome, Alzheimer’s disease and Tourette’s syndrome, metabolic stress, acute brain injury and brain tumors. Micromolar concentrations of S100B can be destructive and pro-apoptotic; they induce the expression of iNOS, COX-2, IL-1, IL‑6 and TNF-alpha by microglia, astrocytes or neurons. Most extracellular actions of S100B can be mediated by RAGE (receptor for advanced glycation end products), which is also a receptor for other S100 proteins... Read More | Purity>97% by SDS-PAGE and HPLC analyses.Additional sequence informationN-terminal Glycine.FunctionChemotactic for monocytes and T-lymphocytes. Binds to CXCR3.Post-translationalCXCL10(1-73) is produced by proteolytic cleavage after secretion from keratinocytes |