Allergen Ingredients TRIZ Cases

Repeated skin allergen application with occlusive patch monitoring promotes immune tolerance while lowering systemic reaction risk.

Peptide-coated bead assays map cow's milk epitopes to diagnose CMA, predict tolerance, and monitor allergic response with less sample.

Purified and recombinant Cupressaceae GRP allergens improve diagnosis of pollen-food cross-reactivity and help identify severe peach allergy risk.

By fully complexing peanut allergens with aluminum, this composition reduces systemic allergic reactions while preserving IgG-driven desensitization.

Mucoadhesive nanofibers and bacterial carriers protect oral mRNA from enzyme degradation and improve delivery for antigen-specific immune tolerance.

Two Ara h 2 peptide epitopes on a solid support improve peanut allergy diagnosis and tolerance monitoring with higher specificity.

Synthetic consensus allergens combine sequences from multiple proteins to desensitize cross-reactive allergies with one broader vaccine approach.

Aqueous extraction with anion exchange and reverse phase chromatography controls Ara h 1, 2, 3, and 6 ratios while limiting aggregates.

Implantable devices co-deliver allergens and AhR agonists to stimulate TGF-β and IL-10, accelerating immune tolerance.

Non-daily maintenance dosing in peanut oral immunotherapy sustains desensitization while easing treatment burden and safety concerns.

Disease-specific antigens are delivered to antigen-presenting cells to induce regulatory T cells without broad immunosuppression or infection risk.

Controlled allergen application on skin uses monitored inflammation to build immune tolerance without adjuvants or routine clinical supervision.

Secretory component shields dimeric IgA-antigen complexes from GI degradation while reducing allergic symptoms.

Peanut immunotherapy uses IgE thresholds to select candidates, tailor monitoring, and reduce adverse reactions during treatment.

Isolating the Cor a 9 allergen protein enables precise detection of hazelnut-induced systemic allergic reactions in patients.

Dry heat sterilization removes replication viable organisms from blended food allergens while maintaining protein structure.

Segmented cockroach allergen peptides modulate specific T cell responses, resolving unaddressed immunopathology in allergic asthma treatments.

Patsnap Eureka analyzes a sesame nsLTP polypeptide immobilized on a solid phase carrier to detect specific IgG and IgE antibodies in patient samples.

Conjugating the IgE Cε3 domain with CRM197 induces protective antibodies that reduce circulating IgE levels and prevent anaphylaxis without adverse reactions.

Baby food products deliver defined allergenic proteins combined with prebiotics to establish long-term immune tolerance and reduce allergy prevalence.

Patsnap Eureka analyzes how purified Equ c s allergen components resolve cross-reactivity issues by distinguishing specific IgE responses from false positives.

Non-aqueous solvent precipitates allergen particles in tissue, resolving unpredictable tolerance induction from traditional aqueous methods.

Conjugating antigens to liver-targeting moieties directs them to hepatocytes, resolving insufficient tolerance induction in autoimmune treatments.

Anti-Ara h 2 antibodies neutralize peanut allergen Ara h 2, preventing IgE binding and anaphylaxis risk during oral immunotherapy.

Segmented pellets with stomach-labile coatings deliver allergens to the gut immune system, reducing false-positive reactions from oral exposure.

A segmented liquid extraction process purifies allergen extracts by sequentially removing lipids and low molecular weight contaminants.

Chitosan and hyaluronic acid bilayers enable controlled protein release through the buccal mucosa, bypassing gastrointestinal degradation.

Acidified ultrafiltration separates flavonoid glycosides from grass pollen extracts, eliminating in vitro genotoxicity while preserving allergen immunogenicity.

Epicutaneous allergen patches bypass injection risks by inducing regulatory T cells, preventing multiple childhood allergies.

Linking mutated Par j 1 and Par j 2 sequences reduces IgE reactivity by 41% and prevents severe side effects in allergic disease immunotherapy.

Dialdehyde crosslinks protein antigens and mannan into a covalent immunogenic complex that stimulates immune responses.

Classifying allergic patients via allergen-specific T cell reactivity measurements to enable customized immunotherapy compositions.

Site-directed mutagenesis creates Mal d 1 variants that lower IgE binding while preserving protective IgG induction to treat pollen and food allergies.

Targeted mutations in the Bet v 1a IgE-binding region reduce IgE reactivity while preserving T-cell epitopes for effective pollen-food syndrome therapy.