| 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 | Purity：>95%(SDS-PAGE) Function：Cooperates with MD-2 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Up-regulates cell surface Purity：>95%(SDS-PAGE) Function：Cooperates with MD-2 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Up-regulates cell surface molecules, including adhesion molecules.Background：CD14 is a 55 kDa cell surface glycoprotein that is preferentially expressed on monocytes/macrophages. The human CD14 cDNA encodes a 375 amino acid (aa) residue precursor protein with a 19 aa signal peptide and a C-terminal hydrophobic region characteristic for glycosylphosphatidyinositol (GPI)-anchored proteins. Human CD14 has four potential N-linked glycosylation sites and also bears O-linked carbohydrates. The amino acid sequence of human CD14 is approximately 65% identical with the mouse, rat, rabbit, and bovine proteins. CD14 is a pattern recognition receptor that binds lipopolysaccharides (LPS) and a variety of ligands derived from different microbial sources. The binding of CD14 with LPS is catalyzed by LPS-binding protein (LBP). The toll-like-receptors have also been implicated in the transduction of CD14-LPS signals. Similar to other GPI-anchored proteins, soluble CD14 can be released from the cell surface by phosphatidyinositol-specific phospholipase C. Soluble CD14 has been detected in serum and body fluids. High concentrations of soluble CD14 have been shown to inhibit LPS-mediated responses. However, soluble CD14 can also potentiate LPS response in cells that do not express cell surface CD14... Read More | Purity≥ 95% SDS-PAGE.Additional sequence informationMature chain.FunctionCould be a growth factor active in the process of wound healing. Acts as a mitogen in the lung. May act in a manner similar to FGF-7 | Purity>97% SDS-PAGE.Interleukin-7 (IL-7) is encoded by the IL7 gene in mouse and secreted by stromal cells in the red marrow and thymus. The protein signals through the IL-7 receptor, which is a heterodimer consisting of IL-7 receptor alpha and IL-2 receptor gamma chain. IL-7 stimulates the Purity>97% SDS-PAGE.Interleukin-7 (IL-7) is encoded by the IL7 gene in mouse and secreted by stromal cells in the red marrow and thymus. The protein signals through the IL-7 receptor, which is a heterodimer consisting of IL-7 receptor alpha and IL-2 receptor gamma chain. IL-7 stimulates the differentiation of hematopoietic stem cells into lymphoid progenitor cells and it can stimulate proliferation of B cells, T cells and NK cells. Mouse IL-7 has approximately 65 % and 88 % amino acid sequence identity with human and rat IL-7 and both proteins exhibit cross-species activity. Recombinant Mouse IL-7 is a 14.9kDa globular protein containing 129 amino acid residues.FunctionHematopoietic growth factor capable of stimulating the proliferation of lymphoid progenitors. It is important for proliferation during certain stages of B-cell maturation... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:Monkeypox is a zoonotic disease caused by monkeypox virus (MPXV), which is a member of orthopoxvirus genus. A35R gene is highly conserved among poxviruses and encodes a previously uncharacterized hydrophobic acidicPurity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:Monkeypox is a zoonotic disease caused by monkeypox virus (MPXV), which is a member of orthopoxvirus genus. A35R gene is highly conserved among poxviruses and encodes a previously uncharacterized hydrophobic acidic protein. The A35R has little homology to any protein outside of poxviruses, suggesting a novel virulence Monkeypox is a zoonotic disease caused by monkeypox virus (MPXV), which is a member of orthopoxvirus genus. A35R gene is highly conserved among poxviruses and encodes a previously uncharacterized hydrophobic acidic protein. The A35R has little homology to any protein outside of poxviruses, suggesting a novel virulence mechanism.A35R could block some stage of antigen processing or presentation in infected cells or interfere with regulation of apoptosis. In addition, the A35R function may be required for growth in certain cell types, e.g., macrophage, in vivo. It localizes to factories where viral DNA is located and it was shown to be a constitutive transcriptional activator in a large-scale yeast two-hybrid study... Read More |