Abstract:
PROBLEM TO BE SOLVED: To provide an improved polymerase composition with optimized performance in a polymerase chain reaction (PCR).SOLUTION: The thermostable DNA polymerase composition completely free from surfactant contains 10-50 mM Tris/HCl, 0.05-0.2 mM EDTA, 0.5-2 mM DTT, 50-200 mM potassium chloride, and 20-80% glycerol.
Abstract translation:待解决的问题:提供在聚合酶链反应(PCR)中具有优化性能的改进的聚合酶组合物。 解决方案:完全不含表面活性剂的热稳定DNA聚合酶组合物含有10-50mM Tris / HCl,0.05-0.2mM EDTA,0.5-2mM DTT,50-200mM氯化钾和20-80%甘油。 版权所有(C)2012,JPO&INPIT
Abstract:
PROBLEM TO BE SOLVED: To provide a method for obtaining a dried composition of reactive compounds, maintaining the living body activity of the compounds on re-dissolving after a certain storage period. SOLUTION: This method for producing the dried composition capable of storing the reactive compounds comprises (a) a process of preparing a liquid composition which is a liquid mixture of the reactive compounds, containing a primer, nucleotide, Taq DNA polymerase and first stabilizing molecule, and (b) a process of drying the liquid mixture by reducing the surrounding pressure of the liquid mixture, wherein, the dried composition of the reactive compounds is dissolvable with an aqueous solution, and the liquid mixture of the reactive compounds in the process (a) contains further an aptamer as a second stabilizing molecule. COPYRIGHT: (C)2010,JPO&INPIT
Abstract:
PROBLEM TO BE SOLVED: To provide an aqueous composition containing a protein having enzymatic activity of an alpha-galactosidase. SOLUTION: This method for stabilizing the aqueous composition containing the protein having the enzymatic activity of the alpha-galactosidase is provided. The method for preparing the purified aqueous composition containing the protein having the enzymatic activity of the alpha-galactosidase is also provided. COPYRIGHT: (C)2011,JPO&INPIT
Abstract:
PROBLEM TO BE SOLVED: To provide an improved variant of T7 RNA polymerase by introducing new mutation leading to improved thermostability of the enzyme.SOLUTION: There is provided a variant of T7 RNA polymerase leading to improved thermostability by introducing a new mutation at positions Val426, Ser633, Val650, Thr654, Ala702, Val795 and combinations thereof.
Abstract:
PROBLEM TO BE SOLVED: To provide a method for amplifying a nucleic acid, by using an amplification reaction for which a primer is used, and to provide a reagent (composition) used in the method. SOLUTION: This composition contains a first modified thermostable enzyme which exhibits 3'-exsonuclease activity but does not substantially exhibit DNA polymerase activity and a second modified thermostable enzyme which exhibits the DNA polymerase activity, wherein the composition is enhanced in enzyme activity, when the enzymes are incubated in an aqueous buffer at an alkaline pH and a temperature of >50°C, so that a primer elongation product is formed. The method for amplifying the target nucleic acid comprises a process (a) where a mixture for the amplification reaction which comprises a primer complementary to the target nucleic acid, deoxynucleotide or its derivative, and the composition is made to contact with a sample and another process (b) where the sample and the mixture for the amplification reaction which are obtained in the process (a) are incubated for such a time at the temperature of >50°C that is enough for reactivating the first and second modified thermostable enzymes and forming the primer elongation product. COPYRIGHT: (C)2003,JPO
Abstract:
PROBLEM TO BE SOLVED: To provide a sufficient amount of a recombinant active heterodimer- AMV-RT. SOLUTION: An active heterodimer-AMV-RT is produced in a prokaryotic host cell by (i) cloning one or more DNA sequences encoding the α-chain and/or the β-chain of AMV-RT to an expression plasmid, (ii) transforming the expressed plasmid to a prokaryotic cell, (iii) inducing a soluble expression of heterodimer-AMV-RT and (iv) isolating the recombinant heterodimer-AMV- RT from the cell.
Abstract:
The present disclosure is directed to the use of certain glycosyltransferase variants having N-terminal truncation deletions. It was found that the combination of two different truncation variants of human ß-galactoside-a-2,6-sialyltransferase I (hST6Gal-I) exhibited different specific sialyltransferase enzymatic activities. In one example, under conditions wherein the first variant ?89 hST6Gal-I catalyzed formation of bi-sialylated target molecules the second variant ?108 hST6Gal-I catalyzed formation of mono-sialylated target molecules. Thus, disclosed are variants of mammalian glycosyltransferase, nucleic acids encoding the same, methods and means for recombinantly producing the variants of mammalian glycosyltransferase and use thereof, particularly for sialylating in a quantitatively controlled manner terminal acceptor groups of glycan moieties being part of glycoproteins such as immunoglobulins.
Abstract:
The present disclosure is directed to the use of certain glycosyltransferase variants having N-terminal truncation deletions. It was found that the combination of two different truncation variants of human ß-galactoside-a-2,6-sialyltransferase I (hST6Gal-I) exhibited different specific sialyltransferase enzymatic activities. In one example, under conditions wherein the first variant ?89 hST6Gal-I catalyzed formation of bi-sialylated target molecules the second variant ?108 hST6Gal-I catalyzed formation of mono-sialylated target molecules. Thus, disclosed are variants of mammalian glycosyltransferase, nucleic acids encoding the same, methods and means for recombinantly producing the variants of mammalian glycosyltransferase and use thereof, particularly for sialylating in a quantitatively controlled manner terminal acceptor groups of glycan moieties being part of glycoproteins such as immunoglobulins.