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

Monoclonal antibody to alpha 2-macroglobulin and its use for detecting glucan

A monoclonal antibody, macroglobulin technology, applied in the field of glucan detection, can solve the problem of not being able to develop analytical glucan and so on

Inactive Publication Date: 2001-01-31
BIOWHITTAKER TECH
View PDF1 Cites 2 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Therefore, the prior art fails to develop a successful method for the analysis of dextran using amebocyte lysate (LAL)

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
  • Monoclonal antibody to alpha 2-macroglobulin and its use for detecting glucan

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0041] This example demonstrates the inhibition of the response of amebocyte lysates to endotoxin but not dextran in the presence of monoclonal antibody 7A10.

[0042] The monoclonal antibody 7A10 was added to the Limulus amebocyte lysate to a final concentration of 1.560 μg / ml, 3, 125 μg / ml, and 6.250 μg / ml. The percentage inhibition of the endotoxin response by the lysate was assessed by measuring the inhibition of the cleavage of the chromogenic substrate in the control lysate without mAb and in the lysate samples spiked with different concentrations of mAb. Each lysate sample was challenged by adding 0.5 Eu / ml endotoxin.

[0043] The response of the lysate sample to this level of endotoxin was completely inhibited when the concentration of mAb 7A10 was 6.250 μg / ml ( figure 1 ). Elevated concentrations of a second mAb, 2D5, which also interacts with Limulus α 2 - specifically binds to one epitope on macroglobulin.

[0044] Addition of purified monoclonal antibody 7A10 c...

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

PropertyMeasurementUnit
purityaaaaaaaaaa
Login to View More

Abstract

The present invention is directed to monoclonal antibodies which specifically bind to a Limulus alpha 2-macroglobulin. Preferred monoclonal antibodies inhibit the enzymatic activation of a Limulus amebocyte lysate to form a gel or to cleave a chromogenic substrate in the presence of an endotoxin but not in the presence of a glucan. The monoclonal antibodies can be used, inter alia, to purify a Limulus alpha 2-macroglobulin, and the preferred antibodies can be used in a method for specifically detecting a glucan in a test sample using an amebocyte lysate.

Description

[0001] technical field of invention [0002] The invention relates to the field of dextran detection. More specifically, the present invention relates to the use of dextran from a Limulus amebocyte lysate. Background of the invention [0003] Limulus amebocyte lysate achieves gel block (gel) formation by two enzymatic pathways. These enzymatic pathways comprise a series of serine proteases that are activated in the presence of endotoxin or dextran, and thanks to this activity, amebocyte lysates are widely used assays to detect the presence of endotoxin. For example in water and biological test samples. [0004] However, it is more sensitive than dextran due to the presence of endotoxin. Therefore, the prior art fails to develop a successful method for the analysis of dextran using amebocyte lysate (LAL). When attempting to detect dextran with amebocyte lysates, the presence of endotoxin in even small amounts in the test sample can lead to false positive results. Therefore...

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 Applications(China)
IPC IPC(8): G01N33/577C07K1/22C07K16/18C07K16/38C07K17/00C12N5/10C12N5/20C12N15/02G01N33/53G01N33/579
CPCC07K16/18Y10S435/975G01N33/5308
Inventor C·J·赫尔布斯特里特M·G·佩佩
Owner BIOWHITTAKER TECH
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