Abstract: Provided is a recombinant KOD polymerase. A KOD polymerase mutant is a protein as follows: the protein is a protein having DNA polymerase activity that is obtained by modifying amino acid residues in at least one of the following 48 positions in the amino acid sequence of KOD DNA polymerase GH78: 267, 326, 347, 349, 353, 375, 378, 379, 380, 385, 451, 452, 453, 454, 457, 461, 465, 470, 474, 477, 478, 479, 480, 482, 484, 485, 486, 493, 496, 497, 514, 574, 584, 605, 610, 630, 665, 666, 667, 674, 676, 680, 682, 698, 707, 718, 723 and 729, without changing other amino acid sequences; and compared with KOD DNA polymerase GH78, with regard to catalysis, the recombinant DNA polymerase exhibits a faster reaction rate, better catalytic efficiency, better affinity and other advantages, thereby improving the reaction rate of DNA polymerase in sequencing and increasing the reaction read length.

Abstract: Provided are a thermostable B-family DNA polymerase mutant and an application thereof. The thermostable B-family DNA polymerase mutant is provided to mutate amino acid residues in at least two of three sites of group A, i.e., 408, 409, and 410 in an amino acid sequence of thermostable B-family DNA polymerases to obtain proteins having DNA polymerase activity. A-group sites (408/409/410), B-group sites (451/485), C-group sites (389/383/384), D-group sites (589/67/680), E-group sites (491/493/494/497), and F-group sites (474/478/486/480/484) of several B-family DNA polymerases are analyzed to design the mutant.

Abstract: Power converters including electronic-embedded transformers for current sharing and load-independent voltage gain are described. In one example, a power converter system includes an input, an output, a power converter between the input and output, and a controller. The converter includes a first bridge, a second bridge, and an electronic-embedded transformer (EET) between the first and second bridge. The EET includes a capacitor and a capacitance coupling switch bridge. The controller generates switching control signals for the first and second bridges and phasing drive control signals for the capacitance coupling switch bridge in the EET. The controller applies a phase shift to the phasing drive control signals for the EET as compared to the switching control signals for the first and second bridges, so that the voltage across the capacitor in the EET cancels the leakage inductance of the transformer windings in the EET, at any switching frequency.

Abstract: The present application relates to a secondary battery, a process for preparing the same and an apparatus containing the same.

Abstract: A chimeric DNA polymerase includes: a first fragment having at least 80% homology to at least part of an N-end domain of KOD DNA polymerase; a second fragment having at least 80% homology to at least part of an exonucleolytic domain of Pab DNA polymerase; a third fragment having at least 80% homology to at least part of the N-end domain of KOD DNA polymerase; a fourth fragment having at least 80% homology to at least part of a palm domain of Pfu DNA polymerase; a fifth fragment having at least 80% homology to at least part of a finger domain of Pab DNA polymerase; a sixth fragment having at least 80% homology to at least part of the palm domain of Pfu DNA polymerase; and a seventh fragment having at least 80% homology to at least part of a thumb domain of KOD DNA polymerase.

Abstract: Provided are a Phi29 DNA polymerase mutant with improved thermal stability and an use thereof in sequencing. The phi29 DNA polymerase mutant is represented by A) or B) below: the DNA polymerase mutant represented by the A) is a protein having DNA polymerase activity that is obtained by modifying at least one amino acid residue(s) in the following six sites in a phi29 DNA polymerase amino acid sequence: the 97-th, 123-th, 217-th, 224-th, 515-th, and 474-th sites; the DNA polymerase mutant represented by the B) is a protein having DNA polymerase activity that is derived from the A) by adding a tag sequence to a terminal of the amino acid sequence of the protein represented by the A).

Abstract: The present disclosure relates to a reverse transcriptase and an application thereof. The reverse transcriptase has mutation sites such as R450H compared with the wild-type M-MLV reverse transcriptase. The reverse transcriptase has increased polymerase activity, improved thermal stability, and reduced RNase H activity.

Abstract: Provided is a recombinant KOD polymerase, which is the following A) or B): the polymerase shown in A) is a protein having DNA polymerase activity that is obtained by modifying amino acid residues in at least one of the following 18 positions in a wild-type KOD DNA polymerase amino acid sequence: 675th, 385th, 710th, 674th, 735th, 736th, 606th, 709th, 347th, 349th, 590th, 676th, 389th, 589th, 680th, 384th, 496th and 383rd; the polymerase described by B) is a protein having DNA polymerase activity that is derived from A) by adding a tag sequence to an end of the amino acid sequence of the protein shown in A).

Abstract: Provided are a group of phi29 DNA polymerase mutants having increased thermal stability and use thereof. The phi29 DNA polymerase mutants are proteins obtained by performing point mutation A and/or point mutation B and/or point mutation C on phi29 DNA polymerase, the point mutation A meaning that an amino acid residue M at position 97 of the phi29 DNA polymerase is mutated to other amino acid residue, the point mutation B meaning that an amino acid residue L at position 123 of the phi29 DNA polymerase is mutated into other amino acid residue, and the point mutation C meaning that an amino acid residue E at position 515 of the phi29 DNA polymerase is mutated to other amino acid residue. The stability of the phi29 DNA polymerase mutants is higher than that of a wild-type phi29 DNA polymerase.

Abstract: Provided are a phi29 DNA polymerase mutant with increased thermo stability, a method for preparing the mutant, the use of the mutant, and a method for increasing the stability of the phi29 DNA polymerase.

Abstract: Disclosed in the present disclosure is a recombinant DNA polymerase. The recombinant DNA polymerase is any one selected from: A) a protein, having amino acid modifications at positions 408, 409 and 485, and at least one of amino acid modification(s) at positions 53, 59, 199, 243, 526, 558, 613, 641, 671, 673, 674, 692 and 709 compared to the amino acid sequence of a wild-type KOD DNA polymerase; B) a protein derived from the protein in A), formed by deleting amino acids 1 to 29 from a C-terminus of the protein in A) and keeping the remaining amino acids unchanged; and C) a protein derived from the protein in A) or B), formed by connecting a tag to the N-terminus or C-terminus of the amino acid sequence of the protein in A) or B), wherein the protein in A), B) and C) has DNA polymerase activity.

Abstract: Provided are a phi29 DNA polymerase and an encoding gene and an application thereof. The phi29 DNA polymerase is C1) or C2): C1) is a protein with DNA polymerase activity obtained by substituting at least one of the 58th, 61st, 94th, 96th, 119th, and 155th amino acid residues in the amino acid sequence of a wild type phi29 DNA polymerase as shown in SEQ ID NO: 2 in the sequence listing; and C2) is a fusion protein obtained by linking a label to the N-terminus and/or C-terminus of the protein represented by C1). A 3?-5?exonuclease of the phi29 DNA polymerase has activity lower than that of the wild type phi29 DNA polymerase, and can efficiently and continuously synthesize DNA during amplification and sequencing.

Abstract: Provided are a group of phi29 DNA polymerase mutants having increased thermal stability and use thereof. The phi29 DNA polymerase mutants are proteins obtained by performing point mutation A and/or point mutation B and/or point mutation C on phi29 DNA polymerase, the point mutation A meaning that an amino acid residue M at position 97 of the phi29 DNA polymerase is mutated to other amino acid residue, the point mutation B meaning that an amino acid residue L at position 123 of the phi29 DNA polymerase is mutated into other amino acid residue, and the point mutation C meaning that an amino acid residue E at position 515 of the phi29 DNA polymerase is mutated to other amino acid residue. The stability of the phi29 DNA polymerase mutants is higher than that of a wild-type phi29 DNA polymerase.

Abstract: Provided are a phi29 DNA polymerase mutant with increased thermo stability, a method for preparing the mutant, the use of the mutant, and a method for increasing the stability of the phi29 DNA polymerase.

Abstract: Provided are a phi29 DNA polymerase and an encoding gene and an application thereof. The phi29 DNA polymerase is C1) or C2): C1) is a protein with DNA polymerase activity obtained by substituting at least one of the 58th, 61st, 94th, 96th, 119th, and 155th amino acid residues in the amino acid sequence of a wild type phi29 DNA polymerase as shown in SEQ ID NO: 2 in the sequence listing; and C2) is a fusion protein obtained by linking a label to the N-terminus and/or C-terminus of the protein represented by C1). A 3?-5?exonuclease of the phi29 DNA polymerase has activity lower than that of the wild type phi29 DNA polymerase, and can efficiently and continuously synthesize DNA during amplification and sequencing.

Abstract: Disclosed in the present disclosure is a recombinant DNA polymerase. The recombinant DNA polymerase is any one selected from: A) a protein, having amino acid modifications at positions 408, 409 and 485, and at least one of amino acid modification(s) at positions 53, 59, 199, 243, 526, 558, 613, 641, 671, 673, 674, 692 and 709 compared to the amino acid sequence of a wild-type KOD DNA polymerase; B) a protein derived from the protein in A), formed by deleting amino acids 1 to 29 from a C-terminus of the protein in A) and keeping the remaining amino acids unchanged; and C) a protein derived from the protein in A) or B), formed by connecting a tag to the N-terminus or C-terminus of the amino acid sequence of the protein in A) or B), wherein the protein in A), B) and C) has DNA polymerase activity.