| Description | DMPK Human Pre-designed siRNA Set A contains three designed siRNAs for DMPK gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components DMPK siRNA-1: 5 nmol (HPLC) DMPK siRNA-2: 5 nmol (HPLC) DMPK siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 DMPK Human Pre-designed siRNA Set A contains three designed siRNAs for DMPK gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components DMPK siRNA-1: 5 nmol (HPLC) DMPK siRNA-2: 5 nmol (HPLC) DMPK 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 | Collagenase NB 1 is chromatographically highly purified; therefore it contains a very high collagenolytic activity. It is largely free from additional enzymatic activities like clostripain, trypsin-like activity and neutral protease, as well as endotoxins.SpecificationsContains chromatographically Collagenase NB 1 is chromatographically highly purified; therefore it contains a very high collagenolytic activity. It is largely free from additional enzymatic activities like clostripain, trypsin-like activity and neutral protease, as well as endotoxins.SpecificationsContains chromatographically highly purified class I and class II collagenase (1).Largely free from clostripain, trypsin-like protease and neutral protease.Vial contains not less than 2000 PZ U collagenase.Activity (Wünsch): ≥ 3.00 U/mgEndotoxin: ≤ 10.0 EU/mg (Ph. Eur.)(Clostridiopeptidase A)EC 3.4.24.3 • Mr ca. 70 000 - 120 000 (collagenases) • CAS [9001-12-1]ApplicationCollagenase NB 1 is, mostly in combination with Neutral Protease NB, suitable for cell isolation from several tissue types.References and DefinitionsUnit definition: Collagenase: 1 U according to Wünsch (2) catalyzes the hydrolysis of 1 µmole 4-phenylazobenzyloxycarbonyl-L-prolyl-L-leucylglycyl-L-prolyl-D-arginine per minute at 25 °C, pH 7.1.Endotoxin: Ph. Eur. (1 Endotoxin Unit is equal to 1 International Unit of a WHO approved reference standard endotoxin (RSE)).References1. Bond, M.D. & van Wart, H.E. (1984) Biochemistry 23, 3077-30912. Wünsch, E. & Heidrich, H.G. (1963) Hoppe-Seyler's Z. Physiol. Chem. 333, 149-51... Read More | 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 | Inquire | Purity:>98%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Heme oxygenase (HMOX) is the rate limiting enzyme in heme catabolism. It cleaves heme to biliverdin, carbon monoxide, and iron. The biliverdin is subsequently converted to bilirubin by biliverdin reductase. Purity:>98%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Heme oxygenase (HMOX) is the rate limiting enzyme in heme catabolism. It cleaves heme to biliverdin, carbon monoxide, and iron. The biliverdin is subsequently converted to bilirubin by biliverdin reductase. The mechanism of HMOX is unique in that heme serves as the substrate of the enzyme and as the prosthetic group for the activation of iron-bound O2. HMOX activity is highest in spleen where senescent erythrocytes are sequestered and destroyed. Two isoforms, HMOX1 and HMOX2, are expressed in most tissues. HMOX1 is an inducible enzyme in response to heme, heavy metals, oxidative stress, cytokines, and many drugs. Whereas HMOX2 displays a constitutive expression. HMOX1 is expressed mainly in spleen, liver, and kidney, and HMOX2 is prominently expressed in the brain and testes. The increased expression of HMOX1 levels is related to a variety of pathological states, where it functions as a cytoprotective molecule through its by products. HMOX1 also plays important roles in the regulation of cell proliferation, differentiation, and apoptosis... Read More |