| Description | Protease S. aureus, V8 (endoproteinase-Glu-C) specifically cleaves peptide bonds on the COOH-terminal side of either aspartic or glutamic acids (Drapeau et al. 1972). Houmard and Drapeau (1972) report that in the presence of ammonium buffers the enzyme specificity can be limited to glutamoyl bonds. Protease S. aureus, V8 (endoproteinase-Glu-C) specifically cleaves peptide bonds on the COOH-terminal side of either aspartic or glutamic acids (Drapeau et al. 1972). Houmard and Drapeau (1972) report that in the presence of ammonium buffers the enzyme specificity can be limited to glutamoyl bonds. Its rather unique specificity, which can be considered as opposite to that of trypsin, makes it a useful tool for protein chemistry and peptide mapping studies (Cleveland et al. 1977) and (Hall et al. 1978).Characteristics of Protease from S. aureus, V8:Characteristics of Protease, Staph aureus (Endoproteinase Glu-C)Molecular Weight27,000 (Drapeau 1978).Optimal pH4.0 and 7.8 with hemoglobin substrate. (Drapeau et al. 1972).Extinction Coefficientextinction coefficient = 4.26 (Houmard 1976).InhibitorsDiisopropyl fluorophosphate (DFP) and monovalent anions such as F-, Cl-, Br-, CH3COO-, and NO3- (Houmard 1976).MethodEnzyme activity is determined by the casein digestion assay described by Drapeau (1976). Since substrate grade caseins can vary from lot to lot and according to the manner produced, the standardization of casein digestion assays has been difficult to achieve. The use of a reference enzyme preparation is suggested. One unit is that amount of enzyme which releases acid soluble fragments equivalent to 0.001 A280 per minute at 37°C and pH 7.8 under the specified conditions.Reagents1% Casein in 0.05 M Tris⋅PO4 buffer, pH 7.8. (Dissolve 1 gram "Hammersten" casein in 50 ml 0.01 N NaOH with gentle heating and stirring. Add 40 ml reagent grade water and 5.0 ml 1.0 M Tris. Adjust pH to 7.8 with H3PO4 and q.s. to 100 ml.)10% Trichloroacetic acid (TCA)EnzymeDissolve at 1 mg/ml in reagent grade water.ProcedureEquilibrate a series of tubes with 5.0 ml of 1% casein at 37°C for 5 minutes. At zero time add 10 ul or 20 ul of enzyme. Mix. Include a reagent blank. Exactly ten minutes after adding sample, stop reaction by adding 5.0 ml TCA. Mix. Allow tubes to stand ten minutes and then filter. Read A280 of the filtrate.Calculation... Read More | Mammalian lactate dehydrogenases (LDH) exist as five tetrameric isozymes composed of combinations of two different subunits. The H subunit predominates in heart muscle, which is geared for aerobic oxidation of pyruvate. The M subunit predominates in skeletal muscle and is concerned more with Mammalian lactate dehydrogenases (LDH) exist as five tetrameric isozymes composed of combinations of two different subunits. The H subunit predominates in heart muscle, which is geared for aerobic oxidation of pyruvate. The M subunit predominates in skeletal muscle and is concerned more with anaerobic metabolism and pyruvate reduction.Catalyzes the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+Recombinant rabbit muscle Lactate Dehydrogenase produced in E.Coli. Chromatographically purified. A lyophilized powder... Read More | Purity> 97 % by SDS-PAGE and HPLC analyses.Additional sequence informationThis product is for the mature full length protein. The signal peptide is not included.FunctionInhibits hemopoiesis and stimulates chemotaxis. Chemotactic in vitro for thymocytes and activated T-cells, but not for B-cells, Purity> 97 % by SDS-PAGE and HPLC analyses.Additional sequence informationThis product is for the mature full length protein. The signal peptide is not included.FunctionInhibits hemopoiesis and stimulates chemotaxis. Chemotactic in vitro for thymocytes and activated T-cells, but not for B-cells, macrophages, or neutrophils. Shows preferential activity towards naive T-cells. May play a role in mediating homing of lymphocytes to secondary lymphoid organs... 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: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining. Function：Actin cross-linking/gelling protein (By similarity). Involved in calcium interactions and contractile properties of the cell that may contribute to replicative senescence |