Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

High stability recombinant procalcitonin and its expression vector and application

A technology of procalcitonin and expression vector, applied in the field of protein, can solve problems such as difficulty in meeting requirements, and achieve the effect of good stability

Active Publication Date: 2022-06-07
GUANGZHOU LDEBIO TECH CO LTD
View PDF7 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0005] CN104610443A discloses a highly stable recombinant procalcitonin, its preparation method and application, which uses the flexible peptide chain linking arms -GG- and -SGGG- to replace the easily degradable 58-59aa, 92-95aa two-part peptide in PCT chain, to obtain highly stable PCT antigen, after 7 days of destruction, the stability of the recombinant PCT is 62.53±0.41%, which is still difficult to meet the requirements in actual use

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
  • High stability recombinant procalcitonin and its expression vector and application
  • High stability recombinant procalcitonin and its expression vector and application
  • High stability recombinant procalcitonin and its expression vector and application

Examples

Experimental program
Comparison scheme
Effect test

Embodiment Construction

[0028] A first aspect of the present invention, providing:

[0029]A recombinant calcitonin proto-calcitonin, the amino acid sequence is: APFRSALESSPADPATLSEDARLLLAALVQDYVMKASELEQEQEREGSSLDSPRSKKCGNLSTCMLGTYTTQDFNKFHTFPQTAIGVGAPGKKKDMSSDLERDHRPHVSMPQNAN.

[0030] In order to better isolate and purify recombinant proteins, in some examples of recombinant calcitonin protogenes, the C or N-terminus is also linked to a protein isolation tag. After isolation and purification, the isolation label can be further removed by enzymatic lysis. Depending on the characteristics of the separation tag, it can be selected to be connected to the C or N end of the recombinant PCT. Separation labels can be a variety of commonly used separation labels, and there are no special requirements in themselves.

[0031] In some examples of recombinant procalcitonin, the protein isolation tag is ligated via a flexible peptide at the C or N-terminus of the recombinant procalcitonin. This is beneficial for rem...

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 highly stable recombinant procalcitonin and its expression vector and application. The amino acid sequence of the recombinant PCT is shown in SEQ ID NO.2. The recombinant procalcitonin of the present invention has good stability and maintains the antigenicity of natural PCT at the same time, and can be used as a PCT standard product replacing natural PCT for detection of PCT antigen concentration.

Description

Technical field [0001] The present invention belongs to the field of proteins, specifically relates to high stability recombinant calcitonin pro and its expression vector and application. Background [0002] PCT (procalcitonin) is an inactive propeptide substance of serum calcitonin (CT), encoded by the Calc-I gene located on chromosome 11 (11p1514), which is generated by selective splicing (encoding 1 to 4 exons), under normal conditions, PCT mRNA is translated into a pre-PCT containing 141 amino acid residues in the coarse endoplasmic reticulum of cells next to thyroid follicles, The molecular mass is 16 kD. The pre-PCT enters the endoplasmic omentum, excises the signal peptide at the N-terminus by glycosylation and specific enzymes, and generates a PCT containing 116 amino acid residues, and in the Golgi body, pcT amino polypeptide (1-57aa), calcitonin (60-91aa) and calcitonin (96-116aa) are finally formed by a series of hydrolases. It can be seen from this that 58-59aa and 92...

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): C07K14/585C07K19/00C12N15/16C12N15/62C12N15/70G01N33/74
CPCC07K14/585C12N15/70G01N33/74C07K2319/21C12N2800/22G01N2333/585
Inventor 杨翔楼建荣黄彬
Owner GUANGZHOU LDEBIO TECH CO LTD
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic, Popular Technical Reports.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com