| Description | Storage buffer: 10mM Tris HCl, 5mM EDTA, 0.03% Bromophenol Blue, 0.03% Xylene Cyanol, 30% Glycerol, pH7.6Product IntroductionThis product is composed of 9 linear double stranded DNA fragments, stored in a 1xLoading Buffer, with dense bands that require high concentration gel and low voltage Storage buffer: 10mM Tris HCl, 5mM EDTA, 0.03% Bromophenol Blue, 0.03% Xylene Cyanol, 30% Glycerol, pH7.6Product IntroductionThis product is composed of 9 linear double stranded DNA fragments, stored in a 1xLoading Buffer, with dense bands that require high concentration gel and low voltage electrophoresis. It is suitable for accurately confirming the size of DNA fragments. The size range is 50-500bp, which are 50bp, 100bp, 150bp, 200bp, 250bp, 300bp, 350bp, 400bp, and 500bp respectively; 250 bp is the bright band, with a concentration 2.5 times that of other bands; In the 5 ul product, each strip contains about 40 ng, and the highlight strip contains about 100 ng.Usage suggestions1. It is recommended to sample 5 ul and increase the sample size appropriately for wide adhesive holes.2. It is recommended to use 2.5-3.5% Agarose or 5% PAGE gel, voltage 4-10 v/cm, and 0.5xTBE buffer for electrophoresis. Pay attention to replacing the electrophoresis buffer in time and using the newly prepared gel to achieve ideal results.3. Stain with EB or other nucleic acid dyes, and observe the electrophoretic bands under UV light.matters needing attention1. This product has been saved in a 1xLoading Buffer and can be directly used for electrophoresis. It is easy to use and the electrophoresis image is clear.2. When using agarose gel containing EB for electrophoretic detection, the bromophenol blue band can be electrophoretic to about 2/3 of the distance, otherwise the small segment will become dark because EB is separated from DNA.3. The accompanying 5xLoading buffer can be used for sample detection.5x Loading Buffer components:10 mM Tris-HCl，5 mM EDTA， pH7.6， 0.03% bromophenol blue, 0.03% xylene blue, 30% glycerol Product componentD745352Component100 T500TStorageD745352ADNA Ladder (50-500bp)500 µL5× 500 µL-20℃. Avoid freeze/thaw cycle.D745352B5xLoading buffer1 mL5× 1 mL-20℃. Avoid freeze/thaw cycle... Read More | Inquire | Biochemical Test:SDS-PAGE (purity > 80%); Western blot with patient sample.Calculated Isoelectric Point:pH 5.68 | 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 | Tyrosine decarboxylase catalyzes the removal of the carboxyl group from tyrosine to produce tyramine and carbon dioxide. Pyridoxal 5'-phosphate is a necessary cofactor. By using the apoenzyme prepared from cells grown on a vitamin B6 deficient medium pyridoxal phosphate may be determined. The Tyrosine decarboxylase catalyzes the removal of the carboxyl group from tyrosine to produce tyramine and carbon dioxide. Pyridoxal 5'-phosphate is a necessary cofactor. By using the apoenzyme prepared from cells grown on a vitamin B6 deficient medium pyridoxal phosphate may be determined. The HOLOenzyme may be used to determine tyrosine, phenylalanine and dihydroxyphenylalanine either manometrically or colorimetrically.L-Tyrosine decarboxylase apoenzyme from Streptococcus faecalis has been used in a study to purify and characterize tyrosine decarboxylase and aromatic-L-amino-acid decarboxylase.L-Tyrosine decarboxylase apoenzyme from Streptococcus faecalis has also been used in a study to investigate the stereospecificity of sodium borohydride reduction of tyrosine decarboxylase... Read More |