| Description | The enzyme is useful for the determination of α-amylase and inorganic phosphate in clinical analysis.PROPERTIESMolecular weight: ca. 34 kDa (gel filtration)Structure: monomer of ca. 25 kDa (SDS-PAGE)Michaelis constant: 2.3×10^−4 M (β-d-glucose-1-phosphate)pH Optimum: ca. 7.0 (The enzyme is useful for the determination of α-amylase and inorganic phosphate in clinical analysis.PROPERTIESMolecular weight: ca. 34 kDa (gel filtration)Structure: monomer of ca. 25 kDa (SDS-PAGE)Michaelis constant: 2.3×10^−4 M (β-d-glucose-1-phosphate)pH Optimum: ca. 7.0 (Fig. 1)pH Stability: 5.0–9.5 (Fig. 2)Optimum temperature: 40°C (Fig. 3)Thermal stability: below 45°C (Fig. 4)Stability (liquid form): stable at 37°C for at least one week (Fig. 5)Stability (powder form): stable at 30°C for at lest one month (Fig. 6)Activators: Mg2+, Mn2+, Co2+, Ni2+Inhibitors: Hg2+, Zn2+, Cu2+, Cd2+STABILIZERS: lactose, EDTAASSAY PROCEDURE PrincipleThe appearance of NADPH is measured spectrophotometrically at 340 nm.ReagentsA. HEPES–NaOH buffer, 0.3 M; pH 7.0, containing 40 mM KCl, 4 mM MgCl2 and 1.6% (w/v) Triton X-100: dissolve 7.15 g of HEPES, 298 mg of KCl, 81.3 mg of MgCl2·6H2O and 1.6 g of Triton X-100 in 75 ml of distilled water, adjust to pH 7.0 with 4 N NaOH and dilute with distilled water to 100 ml.B. d-Glucose-1,6-bisphosphate (G-1,6-P2) solution, 3.0 mM : 60.7 mg of G-1,6-P2 cyclohexylammonium·4H2O/ 25 ml of distilled water.C. NADP+ solution, 12 mM: 230 mg of NADP+·Na/25 ml of distilled water.D. β-d-Glucose-1-phosphate (β-G-1-P) solution, 22 mM:167 mg of β-G-1-P disodium salt/25 ml of distilled water.E. Glucose-6-phosphate dehydrogenase (G6PDH) solution: 1750 U/ml.F. Enzyme dilution buffer: mix 10 mM KH2PO4 solution and 10 mM K2HPO4 solution to make a pH 7.0 solution.Sample: dissolve the lyophilized enzyme to a volume activity of 1.0–3.0 U/ml with ice-cold enzyme dilution buffer (Reagent F) immediately before measurement. Procedure1. Pipette the following reagents into a cuvette (light path: 1 cm).1.5 ml HEPES–NaOH buffer (Reagent A)0.3 ml G-1,6-P2 solution (Reagent B)0.3 ml NADP+ solution (Reagent C)0.3 ml β-G-1-P solution (Reagent D) 0.02 ml G6PDH solution (Reagent E)0.6 ml Distilled water2. Equilibrate at 37°C for about 5 min.3. Add 0.03 ml of sample and mix.4. Record the increase of absorbance at 340 nm in a spectrophotometer thermostated at 37°C, and calculate the ∆Aper min using the linear portion of the curve (∆AS).The blank solution is prepared by adding enzyme dilution buffer (Reagent F) instead of sample (∆A0).CalculationActivity can be calculated by using the following formula:6.2: Millimolar extinction coefficient of NADPH at 340 nm (cm2/µmol)df: Dilution factorC: Content of β-phosphoglucomutase preparation in sample (mg/ml)APPLICATIONSThe enzyme is useful for the determination of α-amylase and inorganic phosphate in clinical analysis.EXPERIMENTAL DATA... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:MCP-2 and CCL7 are two monocyte chemotactic proteins produced by human MG-63 osteosarcoma cells. Both MCP-2 and CCL7 are members of the C-C family of chemokines and share 62% and 71% amino acid sequence identity, Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:MCP-2 and CCL7 are two monocyte chemotactic proteins produced by human MG-63 osteosarcoma cells. Both MCP-2 and CCL7 are members of the C-C family of chemokines and share 62% and 71% amino acid sequence identity, respectively, with MCP-1. CCL7 also shares 58% amino acid identity with MCP-2. CCL7 cDNA encodes a 99 amino acid residue precursor protein from which the N-terminal 23 amino acid residues are cleaved to generate the 76 amino acid residue mature CCL7. Mature CCL7 contains a potential N-linked and several possible O-linked glycosylation sites. Similarly to other C-C chemokines, all three MCP proteins are monocyte chemoattractants. In addition, the three MCPs can chemoattract activated NK cells as well as CD4+ and CD8+ T lymphocytes. All three cytokines have also been shown to attract eosinophils and induce histamine secretion from basophils... Read More | Purity>95% SDS-PAGEFunctionLipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus | Purity> 95% by SDS-PAGE and HPLC analyses.FunctionSerine protease inhibitor that inhibits plasminogen activators and plasmin but not thrombin. May be involved in the formation or reorganization of synaptic connections as well as for synaptic plasticity in the adult nervous system. May protect Purity> 95% by SDS-PAGE and HPLC analyses.FunctionSerine protease inhibitor that inhibits plasminogen activators and plasmin but not thrombin. May be involved in the formation or reorganization of synaptic connections as well as for synaptic plasticity in the adult nervous system. May protect neurons from cell damage by tissue-type plasminogen activator... Read More | Purity>98% by SDS-PAGE and HPLC analyses.Additional sequence informationBelongs to the intercrine alpha (chemokine CxC) family.FunctionActs as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), suggesting that it may be involved in Purity>98% by SDS-PAGE and HPLC analyses.Additional sequence informationBelongs to the intercrine alpha (chemokine CxC) family.FunctionActs as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), suggesting that it may be involved in pathophysiology such as atherogenesis (By similarity). Induces a strong chemotactic response. Induces calcium mobilization. Binds to CXCR6/Bonzo.Post-translationalGlycosylated... Read More |