Thermostable reverse transcriptase

A technology of reverse transcriptase and hydrothermal solution, which is applied to the determination/inspection of transferases, enzymes, microorganisms, etc., and can solve problems such as unsatisfactory thermal stability, demand, and short half-life

Pending Publication Date: 2021-03-05
GUANGDONG FAPON BIOTECH CO LTD
View PDF2 Cites 2 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0003] There are many studies in the prior art through the transformation of reverse transcriptase. After transformation, although the reaction temperature of rever

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Thermostable reverse transcriptase
  • Thermostable reverse transcriptase
  • Thermostable reverse transcriptase

Examples

Experimental program
Comparison scheme
Effect test

Example Embodiment

[0065]Example

[0066]Fusion protein

[0067]The DNA binding protein of the elongated biological or eliminated biological macro group derived from OTG75 ° C is described as an example, and the MMLV is used as an example:

[0068]The amino acid sequence derived from the DNA binding protein SSO7D from Saccharolobus Solfataricus is shown in SEQID NO: 1;

[0069]The amino acid sequence derived from the DNA binding protein PFUD from Pyrococcus Furiosus is shown in SEQ ID NO: 2;

[0070]The amino acid sequence of DNA binding protein TLID from Thermococcus Litoralis is shown in SEQ ID NO: 3;

[0071]The amino acid sequence of DNA binding protein VENTD from the Hydrothermal Vent Metagenome macro-based group is shown in SEQ ID NO: 4.

[0072]2. Fusion of reverse transcriptase and DNA binding protein

[0073]The C-terminal fusion SSO7D obtained by KNMMLV-SSO7D (amino acid sequence is SSO7D (amino acid sequence as SEQ ID NO: 6) The nucleotide sequence is shown as SEQ ID NO: 16); the SSO7D-KNMMLV (the amino acid seque...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

PUM

No PUM Login to view more

Abstract

The invention relates to the technical field of biology, in particular to a thermostable reverse transcriptase to which a DNA binding protein derived from a high-temperature-resistant eosinophile is connected, the thermostability of the reverse transcriptase can be improved, and higher continuous synthesis capacity and template binding capacity are obtained.

Description

technical field [0001] The invention relates to the field of biotechnology, in particular to a thermostable reverse transcriptase. Background technique [0002] Reverse transcriptase is a general term for DNA polymerases that rely on RNA as a template. American scientists H.M.Temin and D.Baltimore discovered reverse transcriptase in 1970, and won the Nobel Prize in Physiology and Medicine in 1975 for this. The discovery of reverse transcriptase has greatly promoted genetic engineering technology. It is an indispensable tool for studying eukaryotic or prokaryotic target genes and constructing cDNA libraries. Together with Taq enzymes, it constitutes the basic tool of modern biotechnology. enzyme. Currently commercialized reverse transcriptases such as MMLV (molomey murine leukemia virus) have limited amplification capabilities, and the length of cDNA fragments generally obtained is not more than 6kb, which is not enough for the construction of cDNA fragments. At the same ti...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

Application Information

Patent Timeline
no application Login to view more
IPC IPC(8): C12N9/12C12N15/54C12Q1/6869
CPCC12N9/1276C12Q1/6869C12Y207/07049C07K2319/00C12Q2521/107C12Q2527/125C12Q2535/122
Inventor 钟淑瑶章瑞程杜翔斐黄杏帆卢庆庆
Owner GUANGDONG FAPON BIOTECH CO LTD
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products