| Description | ANKRD52 Human Pre-designed siRNA Set A contains three designed siRNAs for ANKRD52 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components ANKRD52 siRNA-1: 5 nmol (HPLC) ANKRD52 siRNA-2: 5 nmol (HPLC) ANKRD52 siRNA-3: 5 nmol (HPLC) siRNA ANKRD52 Human Pre-designed siRNA Set A contains three designed siRNAs for ANKRD52 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components ANKRD52 siRNA-1: 5 nmol (HPLC) ANKRD52 siRNA-2: 5 nmol (HPLC) ANKRD52 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 | 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 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>97% SDS-PAGE.FunctionReceptor for interleukin-2 | Purity> 97% (SDS-PAGE&HPLC)Endotoxin level<0.1 EU/µgFunctionProduced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase |