Method for identifying single methylated modification of lysine epsilon-amino group side chain

A lysine residue, lysine technology, applied in the field of detection and diagnosis, can solve problems such as antibody difficulties

Active Publication Date: 2016-01-27
JINGJIE PTM BIOLAB HANGZHOU CO LTD
View PDF3 Cites 10 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

In addition, it is also difficult to prepare antibodies against

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
  • Method for identifying single methylated modification of lysine epsilon-amino group side chain
  • Method for identifying single methylated modification of lysine epsilon-amino group side chain
  • Method for identifying single methylated modification of lysine epsilon-amino group side chain

Examples

Experimental program
Comparison scheme
Effect test

Embodiment Construction

[0059] The present invention uses a specific embodiment to identify or quantify the presence of lysine monomethyl-modified peptides or proteins in cells or tissues, and this enumeration is only exemplary to illustrate how the method of the present invention is implemented, and The present invention cannot be limited in any way. Those skilled in the art can make any improvements and changes to the present invention without departing from the essence of the present invention, but such changes are all included in the scope of the claims of the present invention.

[0060] Example 1: Stable isotope labeling of methionine, in vitro propionylation derivatization and proteolysis

[0061] 1.1 Stable isotope labeling of methionine

[0062] The cells used in the present invention include HeLa cells (cervical cancer cell line), K562 cells (chronic myeloid leukemia cells), SW620 cells (colon cancer cells), A549 cells (lung cancer cells) and SMM7721 cells (hepatoma cells), cultured in R...

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 provides a method for identifying a lysine single methylated modification substrate. The method comprises the following steps: 1) an external acylated derivative reaction is used for deriving a single methylated epsilon-amino group of a substrate protein lysine residue to a propionyl methylated epsilon-amino group; 2) a affinitive enrichment is carried out for peptide fragments with propionyl methylated modification with a pan anti-propionyl methylated lysine antibody prepared by specificity; and 3) a mass spectrum identification is carried out for sites, polypeptide sequences and substrate proteins with propionyl methylated modification after affinitive enrichment by the antibody.

Description

technical field [0001] The present invention belongs to the field of detection and diagnosis, in particular, to a method for identifying and quantifying lysine monomethylation modification substrates in cells or tissues; more particularly, to affinity enrichment and mass spectrometry using specific antibodies A proteomic approach to identify and quantify lysine monomethylation modification substrates in cells or tissues. Background technique [0002] The ε-amino side chains of protein lysine residues can undergo mono-, di-, or tri-methylation modifications. Over the past few decades, biological research on lysine methylation modification (Kme) has mainly focused on core histones. Previous studies have demonstrated the key role of this modification in chromosome structure and function. This modification state is regulated by two groups of enzymes with opposite catalytic functions, lysine methyltransferases and lysine demethylases. Currently, more than 50 lysine methyltrans...

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): G01N33/68
Inventor 程仲毅
Owner JINGJIE PTM BIOLAB HANGZHOU 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