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The post Phanta UC Super-Fidelity DNA Polymerase for Library Amplification (P507) appeared first on SEQRS Kft..

VAHTS Universal Plus Fragmentation, End Preparation & dA-Tailing Module for Illumina V2 is a DNA fragmentation, end repair and dAtailing module optimized for library preparation on Illumina high-throughput sequencing platforms. This kit has been optimized and upgraded from the original version. On the basis of maintaining the original high performance, the ratio of Artificial Invert Chimera Reads in the DNA library of FFPE samples has been significantly reduced, and the reliability of SNV detection has been improved. This kit can efficiently fragment DNA templates from 100 pg to 1 μg and perform end repair, phosphorylation of the 5′ end, and dA tailing of the 3′ end of the fragmented DNA. It significantly reduces the need for starting DNA templates, shortens the experiment time and is compatible with automated library building equipment. All reagents provided in the kit have undergone strict quality control and functional verification to ensure the stability and reproducibility of library preparation to the greatest extent.

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The post VAHTS Universal Plus Fragmentation, End Preparation & dA-Tailing Module for Illumina V2 (N219) appeared first on SEQRS Kft..

Phi29 MAX DNA Polymerase is a DNA polymerase cloned from Bacillus subtilis phage phi29. Phi29 MAX DNAPolymerase has strong strand displacement activity, which can realize the melting and replication of complex DNA structures, and perform isothermal DNA polymerization reactions in vitro that do not rely on thermal cycling. Phi29 MAX DNA Polymerase has strong chain affinity. A single polymerization reaction can achieve continuous polymerization extension up to 100 kb. In addition, Phi29 MAX DNA Polymerase also has a strong 3′-5′ exo-checking activity, which guarantees The fidelity is 1000 times that of Taq enzyme, which is higher than the fidelity of most current high-fidelity enzymes, which guarantees the high fidelity of DNA synthesis, and is very suitable for in vitro preparation of plasmids and complete gene assembly.

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The post Phi29 MAX DNA Ploymerase (N106) appeared first on SEQRS Kft..

Metabolic processes in the body and environmental factors, including oxidation, hydrolysis, deamination, UV irradiation, radiation, and special chemical substances can cause DNA damage. The damage repair mechanism inherent in the body can repair most of the DNA damage, but the DNA damage caused by extraction during the research process will remain on the DNA. If it is not repaired, it will affect the subsequent experiment. VAHTS DNA Damage Repair Kit can be used to repair most DNA damage. The kit contains a variety of enzymes for DNA damage repairing and specially optimized buffer, suitable for a variety of DNA damages, such as apurine/apyrimidine sites, thymine dimers, de-aminocytosine, 8-oxoguanine, oxidized bases, nicks and gaps, deamination cytosine, 3′ terminal half group blocking, etc. This kit can be used to repair formalin fixed paraffin embedding (FFPE) DNA damage and DNA damage caused by various environments or processing methods. But it cannot be used to repair all kinds of DNA damages, such as double-strand breaks and DNA-protein crosslink. This kit can effectively improve the quality of DNA. It has a wide range of compatibility, and the products can be directly used in PCR and second-generation sequencing library construction, third-generation sequencing library construction, etc.

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The post VAHTS DNA Damage Repair Kit (N208) appeared first on SEQRS Kft..

VAHTS Universal Plus Fragmentation, End Preparation & dA-Tailing Module for Illumina is specially designed for Illumina platforms. This kit combines DNA fragmentation, end repair and dA tailing into one step. It is suitable for library preparation from 100 pg – 1 μg of input DNA. With this kit, the input DNA amount is significantly decreased. No mechanical fragmentation of the genome simplifies the process of library construction and shortens the operation time. It is also compatible with automatic library preparation equipment. All the components are subjected to stringent quality control and functional test, ensuring the consistency and reproducibility of library preparation.

The post VAHTS Universal Plus Fragmentation Module (N209) appeared first on SEQRS Kft..

In the presence of templates and primers, T4 DNA polymerase catalyzes the synthesis of DNA along the 5´→3´ direction. This enzyme also has 3´→5´ exonuclease activity, which is stronger than DNA polymerase I. Unlike DNA polymerase I, T4 DNA polymerase does not have 5´→3´ exonuclease activity.

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The post T4 DNA Polymerase (N101-01) appeared first on SEQRS Kft..

T4 Polynucleotide Kinase can catalyze the transfer of the γ-phosphate group of ATP to the 5´-hydroxyl end and 3´-monophosphate nucleoside of the oligonucleotide chain (double-stranded or single-stranded DNA or RNA). T4 Polynucleotide Kinase also has 3´-phosphatase activity, which hydrolyzes 3´-phosphate groups from the 3´ phosphate ends of oligonucleotides, deoxy 3´-monophosphate nucleosides and deoxy 3´-diphosphate nucleosides .

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The post T4 Polynucleotide Kinase (N102-01) appeared first on SEQRS Kft..

T4 DNA Ligase catalyzes the formation of phosphodiester bonds between adjacent 5´-phosphate ends and 3´-hydroxyl ends on double-stranded DNA or RNA. The enzyme not only catalyzes the connection between blunt ends or sticky ends, but also repairs single-strand cuts in double-stranded DNA, RNA, or DNA/RNA hybrids.

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The post T4 DNA Ligase (Rapid) (N103-01) appeared first on SEQRS Kft..

DNA polymerase I, the large fragment (Klenow fragment) is the protease hydrolysate of E. coli DNA polymerase I, with 5´→3´ DNA polymerase activity and 3´→5´ exonuclease activity, but 5 is missing ´→3´ Exonuclease activity. The Klenow fragment retains the high fidelity of the holoenzyme without degrading the 5´ end of DNA.

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The post DNA polymerase I Klenow fragment (N104-01) appeared first on SEQRS Kft..

The Klenow fragment (3´→5´exo-) is the N-terminal truncation of DNA polymerase I. It retains DNA polymerase activity, but loses 5´→3´ exonuclease activity; the enzyme has been mutated ( D355A, E357A) further removed its 3´→5´ exonuclease activity.

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The post DNA polymerase I Klenow fragment exo (N105-01) appeared first on SEQRS Kft..