A variable region sequence of a specific anti-thiamethoxam antibody and its recombinant full-length antibody

A full-length antibody and variable region technology, applied in the field of genetic engineering, can solve problems such as differences between antibody batches, easy loss of effective genes, and inability of cell lines to produce effective antibodies, achieving high selectivity, high sensitivity, and guaranteed recognition active effect

Active Publication Date: 2022-04-19
ZHEJIANG UNIV
View PDF6 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Among the many recombinant antibody expression systems, the mammalian cell expression system can guide the correct folding of recombinant antibodies and provide accurate various post-translational processing and modification functions, so it can stably produce recombinant antibodies with the same activity as the parental antibody, which not only confirms The accuracy of the variable region sequence of the parental antibody can also solve many problems faced by conventional antibody production, such as the batch-to-batch difference of traditional antibodies, and the effective genes are easily lost during the passage and preservation of cell lines, resulting in the inability of cell lines to produce effective antibodies

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
  • A variable region sequence of a specific anti-thiamethoxam antibody and its recombinant full-length antibody
  • A variable region sequence of a specific anti-thiamethoxam antibody and its recombinant full-length antibody
  • A variable region sequence of a specific anti-thiamethoxam antibody and its recombinant full-length antibody

Examples

Experimental program
Comparison scheme
Effect test

Embodiment Construction

[0022] In order to enable those skilled in the art to better understand the solutions of the present invention, the technical solutions in the embodiments of the invention will be clearly and completely described below in conjunction with the drawings in the embodiments of the present invention. Obviously, the described embodiments are only It is a part of embodiments of the present invention, but not all embodiments. Based on the embodiments of the present invention, all other embodiments obtained by persons of ordinary skill in the art without making creative work should belong to the protection scope of the present invention. If there is no special description, the experimental methods in the embodiments are all for the conventional method.

[0023] The anti-thiamethoxam recombinant full-length antibody involved in the present invention includes a heavy chain constant region, a heavy chain variable region, a light chain constant region and a light chain variable region, and...

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 discloses a variable region sequence of a specific anti-thiamethoxam antibody. The amino acid sequence of the heavy chain variable region coding gene is shown in SEQ ID NO:2. The invention also discloses an anti-thiamethoxam recombinant full-length antibody, which includes a heavy chain constant region, a heavy chain variable region, a light chain constant region and a light chain variable region, and the amino acid sequence of the gene encoding the heavy chain variable region is: As shown in SEQ ID NO:2. The invention also discloses an antibody expression plasmid. The sequence genes obtained in the present invention are connected to the expression vectors containing the heavy chain constant region gene and the light chain constant region gene respectively, and the recombinant full-length antibody is obtained by expressing the mammalian cells of the dual-plasmid system, which ensures the stability of the mouse parent antibody. The recognition activity enables the stable production of anti-thiamethoxam antibodies in large quantities, and provides reliable core reagents for various immunoassay methods for the detection of thiamethoxam residues.

Description

technical field [0001] The invention belongs to the technical field of genetic engineering, and in particular relates to the preparation of a variable region sequence of a specific anti-thiamethoxam antibody and a recombinant full-length antibody thereof. Background technique [0002] Neonicotinoid insecticides have become the fastest growing insecticides in the global market and are widely used in more than 120 countries around the world. This type of insecticide inhibits the acetylcholinesterase receptor of the central nervous system of the pest, blocks the normal conduction of the central nervous system of the pest, and causes the paralysis of the pest to death. etc. have a good control effect. Thiamethoxam (3-(2-chloro-1,3-thiazol-5-ylmethyl)-5-methyl-1,3,5-oxadiazin-4-ylidene(nitro)amine) is A second-generation neonicotinoid insecticide with a new structure has strong systemic and osmotic effects, so it will be distributed in various parts of the crop, and because of ...

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
Patent Type & Authority Patents(China)
IPC IPC(8): C07K16/44C12N15/13C12N15/70
CPCC07K16/44C12N15/70C07K2317/56C07K2317/64C07K2317/92C07K2317/33
Inventor 郭逸蓉刘鹏琰赵颖郭源昊焦沙沙柳颖朱国念
Owner ZHEJIANG UNIV
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