Soluble ST2 Antibodies for High-Specificity Detection

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Solution Overview

Problem

Current methods for detecting human soluble ST2 levels are limited in specificity and sensitivity, particularly in distinguishing native from recombinant forms, which affects diagnostic accuracy for inflammatory diseases and cardioprotective mechanisms.

Innovation Solution

Development of antibodies and antigen-binding fragments, such as those produced by hybridomas deposited at the ATCC with designations PTA-10431 and PTA-10432, which specifically bind to human soluble ST2 with high affinity, allowing for competitive binding and improved diagnostic methods for quantitating ST2 levels in samples.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Measurement precision

If current detection methods are used, then detection can be performed, but specificity and sensitivity are limited

Engineering Contradiction:
Improvedetection accuracyVSAvoidspecificity and sensitivity
Core Design Contradiction:
Measurement precisionVSReliability

Solution Approach 1:

The patent develops novel antibodies with optimized binding parameters (affinity, specificity) to detect human soluble ST2. The antibodies are engineered to recognize specific epitopes on the ST2 protein, changing the detection parameters to achieve higher sensitivity and specificity compared to existing methods.

Inventive Principle:
Principle #35Parameter changes

Solution Approach 2:

The patent creates recombinant human soluble ST2 protein copies with native glycosylation patterns to serve as calibration standards and controls. These copied molecules allow for accurate quantitation and validation of the detection assay, improving measurement precision.

Inventive Principle:
Principle #26Copying

2Measurement precision

If existing antibodies are used, then ST2 detection is possible, but difficulty in distinguishing native from recombinant forms reduces diagnostic accuracy

Engineering Contradiction:
Improvediagnostic accuracyVSAvoiddistinguishing native from recombinant forms
Core Design Contradiction:
Measurement precisionVSDifficulty of detecting and measuring

Solution Approach 1:

The patent employs antibodies that recognize specific local epitopes on the ST2 protein structure. By targeting particular regions that are conserved between native and recombinant forms or by recognizing native glycosylation patterns, the assay can distinguish between the two forms and improve diagnostic accuracy.

Inventive Principle:
Principle #3Local quality

Solution Approach 2:

The patent uses a composite detection system combining multiple antibodies with different specificities, recombinant ST2 standards with native glycosylation, and optimized assay conditions. This composite approach enables reliable distinction between native and recombinant ST2 forms.

Inventive Principle:
Principle #40Composite materials

Applied Scientific Principles

This section explains which scientific principles are used to turn an abstract innovation direction into a practical engineering solution.

Function Achieved in This Case

These antibodies and fragments enhance the specificity and sensitivity of ST2 detection, enabling accurate prediction of disease risk, treatment decisions, and clinical study selection based on ST2 levels, improving diagnostic and therapeutic outcomes.

Implementation Method 1

isolated antibodies and antigen-binding fragments thereof that specifically bind to human soluble ST2

Methodology Applied
Scientific EffectAntigen-antibody binding:

Data Source

PatentEP3434694B1Soluble human st-2 antibodies and assays
Publication Date: 2020.12.30 CRITICAL CARE DIAGNOSTICS INC
  • EP3434694B1 patent drawingFigure 1~2
  • EP3434694B1 patent drawingFigure 3A~3B
  • EP3434694B1 patent drawingFigure 3C~4

AI summary

Provided herein are antibodies and antigen-binding antibody fragments that bind to human soluble Growth Stimulation-Expressed Gene 2 (ST2) protein, kits containing these antibodies and antibody fragments, and methods of using these antibodies and antibody fragments.