Anti-Hog TCN1 Antibodies for TCN1 Depletion From HIF

Resolve Bottlenecks,
Find Innovative SolutionsGenerate Solutions

Solution Overview

Problem

There is a lack of commercial sources for anti-hog Transcobalamin I (TCN1) monoclonal antibodies, which are necessary for accurately estimating and removing Hog TCN1 from Hog Intrinsic Factor (HIF) preparations used in vitamin B12 assays, leading to compromised assay integrity due to TCN1 contamination.

Innovation Solution

Development of anti-hog TCN1 monoclonal antibodies, specifically targeting unique peptides on the TCN1 protein, and their use in affinity purification to deplete Hog TCN1 from HIF preparations.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If Hog TCN1 is present in HIF preparations, then the preparation contains the desired Intrinsic Factor protein, but the TCN1 contamination compromises the integrity of B12 assays

Engineering Contradiction:

Improveassay integrityVSAvoidTCN1 contamination

Core Design Contradiction:

ReliabilityVSObject-generated harmful factors

Solution Approach 1:

The patent applies extraction by using anti-Hog TCN1 monoclonal antibodies to specifically bind and remove TCN1 contamination from HIF preparations through affinity purification, thereby eliminating the harmful contaminant while preserving the desired Intrinsic Factor protein

Inventive Principle:

Principle #2Taking out (Extraction)

Solution Approach 2:

The patent uses anti-Hog TCN1 monoclonal antibodies as an intermediary agent that specifically recognizes and binds to TCN1 contamination, enabling its selective removal from HIF preparations without affecting the functional Intrinsic Factor protein

Inventive Principle:

Principle #24Intermediary (Mediator)

2Ease of manufacture

If commercial anti-hog TCN1 monoclonal antibodies are unavailable, then production costs are reduced, but there is no means to estimate or remove TCN1 from HIF preparations

Engineering Contradiction:

Improveavailability of reagentsVSAvoidTCN1 estimation

Core Design Contradiction:

Ease of manufactureVSMeasurement precision

Solution Approach 1:

The patent applies preliminary action by developing and characterizing anti-Hog TCN1 monoclonal antibodies in advance, creating a ready-to-use tool that enables future estimation and removal of TCN1 contamination from HIF preparations without requiring new reagent development each time

Inventive Principle:

Principle #10Preliminary action

3Reliability

If affinity purification with anti-Hog TCN1 antibodies is performed, then TCN1 contamination is reduced to below 0.1% of total protein, but additional purification steps are required

Engineering Contradiction:

Improveassay accuracyVSAvoidpurification process

Core Design Contradiction:

ReliabilityVSDevice complexity

Solution Approach 1:

The patent applies extraction by using affinity purification with anti-Hog TCN1 monoclonal antibodies to specifically remove TCN1 contamination from HIF preparations, achieving reduction to below 0.1% of total protein through targeted extraction of the contaminant

Inventive Principle:

Principle #2Taking out (Extraction)

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

The antibodies effectively reduce Hog TCN1 contamination in HIF preparations to below 0.1% of total protein, ensuring the integrity and accuracy of vitamin B12 assays.

Implementation Method 1

anti-Hog TCN1 monoclonal antibodies that specifically bind to hog transcobalamin-1 (TCN1)

Methodology Applied

Scientific EffectAntigen-antibody binding:

Implementation Method 2

their use in affinity purification to deplete Hog TCN1 from HIF preparations

Methodology Applied

Scientific EffectAffinity purification:

Data Source

PatentUS12509506B2Anti-Hog TCN1 monoclonal antibodies and methods of production and use thereof

Publication Date: 2025.12.30 SIEMENS HEALTHCARE DIAGNOSTICS INC

AI summary

Anti-hog TCN1 monoclonal antibodies are disclosed, along with epitopes recognized by same. Also disclosed are kits containing the monoclonal antibodies and methods of producing the antibodies. Further disclosed are methods of using the monoclonal antibodies, such as (but not limited to) in methods of estimating and/or removing TCN1 from hog intrinsic factor preparations.