| Description | ELOVL2 Human Pre-designed siRNA Set A contains three designed siRNAs for ELOVL2 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components ELOVL2 siRNA-1: 5 nmol (HPLC) ELOVL2 siRNA-2: 5 nmol (HPLC) ELOVL2 siRNA-3: 5 nmol (HPLC) siRNA Negative ELOVL2 Human Pre-designed siRNA Set A contains three designed siRNAs for ELOVL2 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components ELOVL2 siRNA-1: 5 nmol (HPLC) ELOVL2 siRNA-2: 5 nmol (HPLC) ELOVL2 siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 nmol (HPLC) FAM-labeled siRNA Negative Control: 5 nmol (HPLC) GAPDH siRNA Positive Control:5 nmol (HPLC)... Read More | EPOCROSTM is a reactive polymer with an oxazoline group on the side chain and is used as a cross-linking agent for water-based resins. Among the water-based polymers developed to address environmental issues and the increasing use of water-based products due to VOC regulations and desolventing, the EPOCROSTM is a reactive polymer with an oxazoline group on the side chain and is used as a cross-linking agent for water-based resins. Among the water-based polymers developed to address environmental issues and the increasing use of water-based products due to VOC regulations and desolventing, the EPOCROSTM WS series is a “water-soluble type” with the following structure.Features and PropertiesHigher reactivity than water-based epoxy, melamine, blocked isocyanateVOC free (EPOCROS™ WS-300 and EPOCROS™ WS-700)High crosslinking density with a small amount addedOne-pack type with long usage timeImproves water resistance, solvent resistance, heat resistance, and the strength of films, etc.Adhesion-imparting possible to PET, OPP, PVC, etc.Fast dryingLow toxicity (Ames Test: Negative, Primary Skin Irritation Test: No irritation)WS Series Product LineupApplicationsNonwoven fabric bindersPigment printingCoatings (metals, films, leather)Paint and coatings, Primers (plastics, building materials, vehicles)AdhesivesMethodASSAY for Product Code DILW:One unit equals a decrease in absorbance of 1.0 per minute at 25°C at pH 7.5 with 2,6-dichlorophenolindophenol as the chromogen.Reagents0.2 M Tris⋅HCl buffer, pH 7.50.006 M NADH. Prepare fresh daily.0.0012 M Dichlorophenolindophenol (DCPIP) Prepare fresh daily.EnzymePrepare a 10 mg/ml solution of enzyme in 0.2 M Tris⋅HCl, pH 7.5.Dilute further immediately before use to give ΔA/min of 0.15-0.20.ProcedureAdjust spectrophotometer to 600 nm and 25°C.Pipette into cuvettes as follows:Mix quickly and measure the decrease in absorbance at 600 nm for 2-3 minutes.Determine the ΔA/min. from the initial linear portion of the curve. (Use portion of curve from t=0 to t=1 minute; the rate is linear for 1/2 to 1 minute.)Calculation... Read More | Seals and prevents freezing of stopcocks and ground-glass joints in high-vacuum systems at pressures less than 10-6 mm Hg. Heat stable (?40 to 260 °C), low vapor pressure, and chemically resistant. Colorless. 5.3 oz. tube | TEV Protease is the 241 amino acid (aa), 27 kDa catalytic domain of the nuclear inclusion a (NIa) protein encoded by the potyvirus, tobacco etch virus (TEV). It may be used in biotechnology to cleave affinity tags from recombinant proteins, either co-translationally orin vitrofollowing purification.TEV Protease is the 241 amino acid (aa), 27 kDa catalytic domain of the nuclear inclusion a (NIa) protein encoded by the potyvirus, tobacco etch virus (TEV). It may be used in biotechnology to cleave affinity tags from recombinant proteins, either co-translationally orin vitrofollowing purification. Its high specificity and activity at a wide range of pH and ionic strength make TEV Protease more versatile than many other proteases used for the same purpose. Unlike factor Xa, enteropeptidase or thrombin, TEV Protease has not been found to cleave at unintended sites, even when present at a high concentration. TEV Protease is a 3C-type protease that cleaves substrates with a consensus sequence of ENLYFQG. Cleavage occurs between Q and G. Since the final aa remains on the cleaved protein where it could potentially affect structure or function, substitution of a variety of aa have been tested. In order of efficiency, S, A, M, Y, D, N, E, K or L may be effectively used in place of G. Several of the remaining aa may also vary, giving a final consensus sequence of ExxYF(M)Q(E)/G(S, A or others) where aa in parenthesis are alternatives and x is any aa. The autocatalytic site of NIa at S2256 has been mutated to an N for improved stability of the protease.Tobacco Etch Virus Protease is a highly site-specific cysteine protease that is found in the tags from fusion proteins. The optimal temperature for cleavage is 30°C. It is recommended that the cleavage for each fusion protein be optimized by varying the amount of recombinant viral TEV protease, reaction time, or incubation temperature. It can be removed by Ni2+ affinity resin... Read More | Purity>97% by SDS-PAGE and HPLC analyses.Additional sequence informationFunction N-terminal glycine. Full-length mature chain lacking the signal peptideFunctionHas chemotactic activity for neutrophils. May play a role in inflammation and exerts its effects on endothelial cells in an autocrine Purity>97% by SDS-PAGE and HPLC analyses.Additional sequence informationFunction N-terminal glycine. Full-length mature chain lacking the signal peptideFunctionHas chemotactic activity for neutrophils. May play a role in inflammation and exerts its effects on endothelial cells in an autocrine fashion. In vitro, the processed forms GRO-alpha(4-73), GRO-alpha(5-73) and GRO-alpha(6-73) show a 30-fold higher chemotactic activity.Post-translationalN-terminal processed forms GRO-alpha(4-73), GRO-alpha(5-73) and GRO-alpha(6-73) are produced by proteolytic cleavage after secretion from peripheral blood monocytes... Read More |