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

Recombination human Mucl-MBP fusion protein antitumour vaccine and production technology

A fusion protein, anti-tumor technology, applied in the field of recombinant human MUC1-MBP fusion protein anti-tumor vaccine, can solve problems such as weak immunogenicity and toxic T cells

Inactive Publication Date: 2004-07-21
台桂香
View PDF0 Cites 21 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Most of the fusion protein vaccines developed in the past are artificially synthesized polypeptides, and most of them face the disadvantages of weak immunogenicity and inability to induce cytotoxic T cells (CTL).

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
  • Recombination human Mucl-MBP fusion protein antitumour vaccine and production technology
  • Recombination human Mucl-MBP fusion protein antitumour vaccine and production technology
  • Recombination human Mucl-MBP fusion protein antitumour vaccine and production technology

Examples

Experimental program
Comparison scheme
Effect test

Embodiment

[0097] 1. Construction of MUC1-MBP fusion protein expression vector

[0098] 1. Routine plasmid extraction and purification. (See Molecular Cloning Experiment Guide, J. Sam Brook, edited by Science Press, 1998)

[0099] 2. Separation and recovery of digested fragments.

[0100] (1) Digest pMAL-P2 and PSK-MUC1 plasmids with EcoRI and HindIII for 1-3 hours at 25-37°C.

[0101] (2) The DNA fragments were separated by electrophoresis on 0.7-1.5% agarose gel, and the vector fragment pMAL-p2 and the 450bp target fragment MUC1 were recovered by a freeze-thaw method or a kit.

[0102] (3) Electrophoresis on 0.7-1.5% agarose gel to identify the recovered carrier fragment and target fragment.

[0103] 3. Ligation of pMAL-p2 vector and MUC1 fragment

[0104] pMAL-p2 vector fragment 1-10μl

[0105] MUC1 fragment 5-20μl

[0106] EcoRI 2-4μl

[0107] HindIII 2-4μl

[0108] T4 ligase 1-2μl

[0109] According to the above amount, react overnight at 16°C in a 50-100 μl reaction system....

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

An anticancer vaccine of recombinant human MOC1-MBP fusion protein is disclosed, in which MBP is used as its adjuvant. The MBP gene and MUC1 gene are fused together. The MBP substituted for other fusion protein to induce CTL reaction. The pMAL-P2 is the carrier for effectively expressing maltose fusion protein. The serial repetitive sequence of MUC1 is inserted to downstream of malE gene.

Description

Technical field: [0001] The present invention relates to the vaccine technology of active and specific immunity in tumor biological treatment, especially provides a recombinant human MUC1-MBP fusion protein anti-tumor vaccine and its production process, so as to achieve the purpose of preventing and treating tumors, and belongs to the technical field of genetic engineering fusion protein . Background technique: [0002] MUC1 is an important member of the Mucin family of mucins, present on the surface of normal ductal epithelial cells and their derived tumor cells, and consists of a polypeptide core (core peptide) and side branch sugar chains. Normal tissue MUC1 is different from tumor tissue. The former is distributed in the secretory pole of ductal epithelial cells, relatively isolated from immune cells, and rich in glycosylation; while the latter is widely distributed and abnormally abundantly expressed on the surface of cancer cells, and glycosylation is incomplete. Epit...

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): A61K38/39A61K39/00A61K45/00C12N15/62
Inventor 台桂香
Owner 台桂香
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