| Description | Product IntroductionGlucose oxidase is a well-characterised flavoprotein that catalyses oxidation of β-D-Glucose at its first hydroxyl group, utilizing molecular oxygen as the electron acceptor, to produce D-glucono-delta-lactone and hydrogen peroxide. Glucose oxidase is a homodimeric enzyme, Product IntroductionGlucose oxidase is a well-characterised flavoprotein that catalyses oxidation of β-D-Glucose at its first hydroxyl group, utilizing molecular oxygen as the electron acceptor, to produce D-glucono-delta-lactone and hydrogen peroxide. Glucose oxidase is a homodimeric enzyme, with an FAD molecule moncovalently but tightly bound at the active site of each 80 KDa subunit. The enzyme consists of two identical polypeptide chain subunits (80,000 Daltons) covalently linked by disulfide bonds. Each subunit contains one mole of Fe and one mole of FAD (flavin-adenine dinucleotide). The molecule consists of approximately 74% protein, 16% neutral sugar and 2% amino sugars. The FAD is replaceable with FHD (flavin-hypoxanthine dinucleotide) without loss of activityDiagnostic applicationGlucose oxidase can be utilized in the enzymatic determination of D-glucose in solution. As glucose oxidase oxidizes β-D-glucose to D-gluconolactate and hydrogen peroxide, horseradish peroxidase is often used as the coupling enzyme to visualize colorimetrically the formed hydrogen peroxide for the rapid determination of free glucose in samples. Enzymatic glucose biosensors use an electrode instead of O2 to take up the electrons needed to oxidize glucose and produce an electronic current in proportion to glucose concentration, which is the technology behind the disposable glucose sensor strips used by diabetics to monitor serum glucose levels.Food industry applicationsGlucose oxidase assay allows the monitoring of glucose levels in fermentation and bioreactors. It also helps food preservation by removing oxygen from food, wine, beer packaging and bottling. Glucose oxidase is widely used to remove residual glucose to inhibit non-enzymatic browning... Read More | Inquire | Biochemical Test:SDS-PAGE (purity > 80%); Western blot with patient sample.Calculated Isoelectric Point:pH 4.19 | Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：CNN1 is a member of the calponin family. CNN1 is a thin filament-associated protein which is involved in the regulation and modulation of smooth muscle contraction. CNN1 is able to bind to actin, calmodulinPurity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：CNN1 is a member of the calponin family. CNN1 is a thin filament-associated protein which is involved in the regulation and modulation of smooth muscle contraction. CNN1 is able to bind to actin, calmodulin, troponin C and tropomyosin. Prevention of actomyosin Mg-ATPase activity is a result of interaction between calponin and actin... Read More | Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： CD4, also known as L3T4, T4, and W3/25, is an approximately 55 kDa type I transmembrane glycoprotein that is expressed predominantly on thymocytes and a subset of mature T lymphocytes. It is a standard Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： CD4, also known as L3T4, T4, and W3/25, is an approximately 55 kDa type I transmembrane glycoprotein that is expressed predominantly on thymocytes and a subset of mature T lymphocytes. It is a standard phenotype marker for the identification of T cell populations. Mature human CD4 consists of a 371 amino acid (aa) extracellular region containing four immunoglobulin-like domains, a 22 aa transmembrane segment, and a 40 aa cytoplasmic domain. Within the ECD, human CD4 shares approximately 52% aa sequence identity with mouse and rat CD4. CD4 is expressed along with CD8 on double positive T cells during their development in the thymus. Either CD4 or CD8 expression is then lost, giving rise to single positive (SP) CD4+ or CD8+ mature T cells. CD4+ SP cells, also known as T helper cells, further differentiate into multiple subsets of CD4+ cells including Th1, Th2, Th17, Tfh, and Treg cells which regulate humoral and cellular immunity. CD4 is reexpressed on circulating CD8+ T cells upon activation and contributes to their cytotoxic effector activity. In human, CD4 is additionally expressed on macrophages, neutrophils, monocytes, NK cells, and neurons and glial cells in the brain. Similar CD4 distribution between species cannot be assumed as demonstrated by its presence on macrophages in human and rat but not in mouse. CD4 binds directly to MHC class II molecules on antigen presenting cells. This interaction contributes to the formation of the immunological synapse which is focused around the TCR-MHC class II-antigenic peptide interaction. Palmitoylation of two cysteine residues in the cytoplasmic tail of CD4 promotes the localization of CD4 in lipid rafts and its ability to augment TCR signaling via activation of the tyrosine kinase Lck. CD4 also functions as a chemotactic receptor for IL-16 and, in human, as a co-receptor for the gp120 surface glycoprotein of HIV-1... Read More |