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Fel d 1

Fel d 1 is the major allergen secreted by domestic cats (Felis catus), a small glycoprotein belonging to the secretoglobin superfamily that elicits IgE-mediated hypersensitivity reactions in up to 95% of individuals with cat allergy.^[1]^[2] Structurally, it forms a compact, all-helical tetramer of approximately 35–38 kDa, consisting of two disulfide-linked heterodimers each made from chain 1 (70 amino acids, ~8 kDa) and chain 2 (85–92 amino acids, ~10 kDa), with an internal cavity and two calcium-binding sites.^[1]^[3] Produced primarily in sebaceous glands and also in salivary and anal glands, Fel d 1 is transferred to fur and dander during grooming, rendering it highly airborne and persistent in environments, with concentrations detectable in up to 99.9% of homes.^[1]^[2] The biological function of Fel d 1 remains unclear, though it may serve as a carrier for lipids, steroids, or pheromones, or contribute to skin protection and immune modulation akin to other secretoglobins like uteroglobin.^[1]^[4] Encoded by two linked genes on chromosome A1 (CH1 and CH2), it exhibits isoforms due to variations in chain 2 length, with higher production in intact male cats compared to females or neutered males.^[4]^[1] As the dominant cat allergen, Fel d 1 accounts for 60–90% of the total IgE reactivity to cat dander and is recognized by mannose receptors on antigen-presenting cells, promoting a Th2-biased immune response that correlates with asthma severity in sensitized individuals.^[1]^[2] Its thermostability and adhesion to small particles (<5 μm) facilitate widespread dispersal, contributing to sensitization rates of 10–30% in the general population and 20–40% among atopics.^[1] Ongoing research focuses on mitigating Fel d 1's allergenicity, including recombinant forms for diagnostics and immunotherapy, peptide vaccines, and genetic engineering via CRISPR-Cas9 to knock out chain 2 expression, yielding hypoallergenic cats with over 98% reduced salivary Fel d 1 levels (as demonstrated in 2024 studies, with 2025 research further confirming feasibility through CH2 knockouts in feline cells).^[1]^[4]^[5]^[6] These advances highlight Fel d 1's central role in cat allergy management, affecting an estimated 10–20% of the global population with pet allergies.^[1]^[2]

Discovery and Characterization

Initial Identification

The identification of Fel d 1 as the primary cat allergen emerged in the early 1970s through investigations into cat dander and pelt extracts using skin prick tests to assess allergic responses in sensitized individuals.^[7] Early work focused on extracting and characterizing components from cat pelts, revealing a dominant allergenic fraction responsible for most reactions in cat-allergic patients.^[8] Researchers such as Francis C. Lowell and Jack L. Ohman Jr., in collaboration with Kurt J. Bloch, pioneered these efforts, with a 1973 study detailing the extraction process and initial biochemical properties of the allergen from cat sources.^[7] By the mid-1970s, the advent of radioallergosorbent tests (RAST) enabled more precise detection of IgE antibodies specific to cat allergens, confirming the major component's role in hypersensitivity.^[9] Ohman and Lowell's 1977 study quantified IgE binding in an allergic population, demonstrating that this dominant allergen elicited responses in the majority of cat-sensitive individuals, laying the groundwork for its recognition as the principal mediator of cat allergy.^[9] These findings highlighted the allergen's prevalence, with subsequent early analyses showing it accounted for 60-90% of cat-specific IgE responses among affected patients.^[10] Isolation and purification advanced in the 1970s using techniques such as gel filtration chromatography on Sephadex columns and ion-exchange chromatography on DEAE-cellulose, which separated the major allergen from crude extracts for detailed study.^[8] These methods allowed for partial purification, enabling antigenic and allergenic characterization that solidified its status.^[11] In 1988, the International Union of Immunological Societies (IUIS) formally designated it as Fel d 1, standardizing nomenclature for this secretoglobin-like protein and facilitating global research consistency.^[12]

Biochemical Classification

Fel d 1 belongs to the secretoglobin superfamily, a group of small, secreted proteins also known as uteroglobin-like proteins, which are characterized by their compact structures and roles in modulating inflammatory responses.^[13] As a tetrameric glycoprotein, Fel d 1 exhibits a molecular weight of approximately 35-38 kDa, consisting of two disulfide-linked heterodimers each formed by chain 1 (α-chain) and chain 2 (β-chain).^[14] This classification underscores its evolutionary relation to other secretoglobins, such as rabbit uteroglobin, which shares structural similarities despite functional differences. The protein is encoded by two distinct genes: CH1, which produces the α-chain, and CH2, which produces the β-chain. These genes are located in close proximity on feline chromosome E2, within a region spanning less than 10,000 base pairs, facilitating coordinated expression.^[15] The CH1 gene comprises three exons separated by two introns, while the CH2 gene structure supports the production of two isoforms—a long form of 92 amino acids preferentially expressed in salivary glands and a short form of 90 amino acids—through alternative processing.^[6]^[16] Post-translational modifications are essential for Fel d 1's stability and function, including N-linked glycosylation primarily at asparagine residue 33 (Asn33) in the β-chain (chain 2), which contributes to structural heterogeneity via variable glycan attachments.^[17] Additionally, three interchain disulfide bonds covalently link the chains within each heterodimer, forming the mature tetrameric structure and enhancing resistance to denaturation.^[4] Fel d 1 is an acidic protein with an isoelectric point (pI) of approximately 5.0, which promotes its solubility in salivary and sebaceous secretions where it is predominantly found.^[18] This low pI reflects its high content of negatively charged residues, aiding in its dispersal and persistence in the environment.^[19]

Molecular Structure

Protein Composition

Fel d 1 is a heterodimeric protein composed of two distinct polypeptide chains, designated chain 1 (also known as α or CH1) and chain 2 (β or CH2), which are encoded by separate genes and covalently linked by three interchain disulfide bonds.^[1] Each chain is synthesized as a precursor with an N-terminal signal peptide that is cleaved during maturation, yielding the functional mature proteins. In its native state, the heterodimer often assembles into dimers or tetramers through non-covalent interactions, resulting in a glycoprotein complex with an overall molecular weight of approximately 35-38 kDa.^[3] Chain 1 comprises 70 amino acids and has a molecular weight of about 8 kDa, featuring conserved cysteine residues that contribute to structural integrity.^[10] Chain 2 is slightly larger, consisting of 92 amino acids (though natural forms may include truncated variants of 85 or 90 residues) with a molecular weight of approximately 10 kDa, and it shares structural motifs with chain 1, including positions for disulfide linkage.^[1] The disulfide bridges critical for heterodimer stability are formed between Cys3 of chain 1 and Cys73 of chain 2, Cys44(1) and Cys48(2), and Cys70(1) and Cys7(2).^[20] Sequence analysis of Fel d 1 from domestic cats reveals polymorphisms leading to isoform variability, with over 30 unique amino acid substitutions documented, including more than 20 distinct variants.^[21] Despite this diversity, the core amino acid sequence is highly conserved across individuals, exhibiting 92-99% identity, which underscores the protein's functional consistency as a major allergen.^[22]

Three-Dimensional Conformation

Fel d 1 exhibits a compact globular fold typical of the secretoglobin family, forming a tetramer composed of two non-covalently associated heterodimers, with each heterodimer consisting of chain 1 (70 amino acids) and chain 2 (85–92 amino acids) covalently linked by three interchain disulfide bonds.^[23] Each chain adopts an all-α-helical structure with four α-helices that pack together to create a hydrophobic core, providing structural stability essential for the protein's function as an allergen.^[23] This helical bundle arrangement results in a compact monomer-like unit per heterodimer, with the overall tetrameric assembly reaching a molecular weight of approximately 35–38 kDa.^[24] The three-dimensional structure of Fel d 1 was elucidated through X-ray crystallography, with a seminal study reporting the atomic model of a recombinant heterodimer mimic (chains 2 and 1 fused without a linker) at 1.85 Å resolution using multi-wavelength anomalous diffraction on selenomethionine-substituted protein.^[23] This high-resolution structure reveals eight α-helices in total (four per chain), an internal asymmetric cavity potentially capable of binding amphipathic ligands such as steroids or fatty acids, and surface-exposed regions critical for immunological interactions.^[23] Subsequent refinements, including a 1.64 Å structure of the natural heterodimer (PDB ID: 1ZKR), confirm the helical packing and disulfide connectivity, with cysteines at positions 3, 44, and 70 in chain 1 forming bonds to Cys73, Cys48, and Cys7 in chain 2, respectively.^[25] The interface between the two heterodimers in the tetrameric form is primarily stabilized by hydrophobic interactions involving non-polar residues from the helical surfaces, enhancing the protein's environmental persistence and resistance to denaturation.^[24] This quaternary arrangement buries significant surface area, approximately 1,200 Å² per interface, which contributes to the overall compactness and may modulate accessibility of functional sites.^[26] The tetrameric structure also features two calcium-binding sites: one external site symmetrically positioned on each side of the tetramer and another within the dimerization interface, contributing to stability.^[27] Epitope mapping has localized key IgE-binding sites to exposed loops on the protein surface, with major conformational epitopes identified in residues 25–38 (VAQYKALPVVLENA) and 46–59 on chain 1, and residues 15–28 on chain 2.^[28] The crystal structure positions these epitopes prominently on the exterior, away from the hydrophobic core and dimer interface, facilitating antibody recognition while the helical fold and disulfides maintain structural integrity during immune encounters.^[23] These surface features underscore the role of the three-dimensional conformation in Fel d 1's allergenicity, as disruptions to the fold can alter epitope exposure and IgE affinity.^[28]

Production and Variation in Cats

Sites of Synthesis

Fel d 1 is primarily synthesized in the submandibular and sublingual salivary glands, sebaceous glands of the skin, and anal sacs of domestic cats, with these sites accounting for the majority of the allergen's production.^[29] Sebaceous glands represent the predominant source, contributing to direct secretion through skin oils, while salivary production occurs mainly in the sublingual glands.^[30] Anal sacs also serve as a significant reservoir, with Fel d 1 levels detected at high concentrations in their secretions.^[31] Minor synthesis takes place in the lacrimal glands, where Fel d 1 concentrations in lacrimal fluid are comparable to those in saliva, ranging from 6.8 to 14 units per milliliter.^[32] Following synthesis, Fel d 1 is secreted into saliva, facilitating its transfer to the fur and dander during grooming behaviors, which spreads the allergen across the cat's coat.^[30] Sebaceous gland-derived Fel d 1 is released directly onto the skin surface via sebum, embedding in the epidermis and hair shafts.^[33] At the cellular level, expression occurs predominantly in glandular epithelial cells, including sebaceous cells within skin glands and squamous epithelial cells in associated tissues.^[33]

Factors Influencing Levels

The production of Fel d 1 in cats exhibits notable sexual dimorphism, with intact male cats generally producing higher levels than females due to hormonal regulation by testosterone. Studies have shown that male cats secrete significantly more Fel d 1 than female cats, primarily originating from skin sources. Neutering intact males leads to a substantial reduction in Fel d 1 production, with levels decreasing to approximately one-third to one-fifth of pre-neutering amounts, corresponding to a 67-80% drop in output. This hormonal influence underscores the role of androgens in modulating allergen expression, though specific promoter elements remain under investigation. Breed-specific differences also contribute to variability in Fel d 1 levels, with certain breeds demonstrating inherently lower production due to genetic factors. For instance, Siberian cats often exhibit reduced Fel d 1 secretion compared to other breeds, with about 50% of individuals producing lower levels and roughly 15% showing exceptionally low amounts, attributed to polymorphisms in the CH1 and CH2 genes that encode the allergen. Similarly, Russian Blue cats are noted for lower Fel d 1 output linked to their genetic makeup, making them relatively hypoallergenic. These variations arise from sequence differences in the Fel d 1 genes, with up to 58% amino acid variability in the CH2 chain across populations, enabling selective breeding for reduced allergenicity. Age and seasonal factors further influence Fel d 1 levels over time. Younger cats, particularly young adults, tend to produce higher salivary Fel d 1 concentrations than older individuals, with levels declining as cats age. Seasonally, Fel d 1 peaks during winter and spring, coinciding with breeding periods when hormonal fluctuations may enhance production, though levels remain relatively stable year-round in neutered cats. Individual cats also display consistent "low-shedder" profiles, driven by genetic heritability, as evidenced by high inter-cat variability and familial patterns in allergen output, with studies estimating a moderate genetic component to production differences.

Allergenicity in Humans

Immunological Response

Fel d 1 elicits an IgE-mediated type I hypersensitivity reaction in sensitized individuals, where the allergen binds to IgE antibodies already attached to the high-affinity FcεRI receptors on the surface of mast cells and basophils.^[34] This binding cross-links adjacent IgE-FcεRI complexes, triggering intracellular signaling cascades that lead to rapid degranulation of these cells, releasing preformed mediators such as histamine, as well as newly synthesized cytokines like IL-4, IL-5, and IL-13.^[1] The histamine release contributes to immediate symptoms, while cytokines amplify the inflammatory response by promoting eosinophil recruitment and further IgE production. The sensitization process begins with exposure to Fel d 1 through inhalation or skin contact, where the allergen is taken up by antigen-presenting cells (APCs), such as dendritic cells, via mannose receptors.^[30] Within APCs, Fel d 1 is processed into peptides and presented on MHC class II molecules to naïve T cells, preferentially driving differentiation into Th2 cells in genetically susceptible individuals.^[34] Th2 cells then secrete cytokines including IL-4 and IL-13, which stimulate B cells to undergo class-switch recombination and produce Fel d 1-specific IgE antibodies that circulate and bind to FcεRI on effector cells, priming them for future encounters with the allergen.^[30] Cross-reactivity of Fel d 1 with other allergens is generally limited among secretoglobins but has been observed with certain components in dog dander, such as a 20 kDa protein that shares IgE-reactive epitopes, potentially due to conformational similarities.^[35] This cross-reactivity may explain dual sensitization in some patients allergic to both cats and dogs, although it does not extend broadly to the major dog allergen Can f 1.^[36] The dose-response relationship for Fel d 1 involves airborne concentrations below 100 ng/m³ sufficient to provoke reactions in sensitized individuals, with higher levels correlating to more severe responses.^[34] The affinity of IgE for Fel d 1 is in the sub-nanomolar range (Kd ≈ 10^{-9} M), enabling efficient cross-linking even at low allergen doses.^[37]

Clinical Impact

Fel d 1 is the primary allergen responsible for cat allergy, affecting 10-20% of the global population in regions with high cat ownership rates.^[38] Among individuals allergic to cats, 80-95% exhibit sensitization specifically to Fel d 1, as measured by detectable IgE antibodies.^[2] This high sensitization rate underscores Fel d 1's dominant role in eliciting allergic responses to cats. The most common clinical manifestations of Fel d 1 sensitization include rhinoconjunctivitis, characterized by nasal congestion, sneezing, and itchy, watery eyes, as well as asthma exacerbations such as wheezing, shortness of breath, and cough.^[39] Atopic dermatitis may also occur, presenting as itchy, inflamed skin or hives upon exposure.^[40] Severe reactions like anaphylaxis are rare in cat allergy.^[41] Diagnosis of Fel d 1 allergy relies on skin prick tests using Fel d 1 extracts, where a wheal diameter greater than 3 mm indicates positivity, confirming sensitization in symptomatic patients.^[42] Serum-specific IgE testing via ImmunoCAP assay is also standard, with levels above 0.35 kU/L denoting clinically relevant sensitization to Fel d 1.^[43] Early-life exposure to Fel d 1 has a complex relationship with sensitization risk; while some cohort studies show higher rates among infants in cat-owning households, recent analyses suggest no increased risk or even protective effects against asthma development.^[44]^[45] Sensitization to Fel d 1 is associated with elevated asthma development, with an odds ratio of 2.6 (95% CI 1.27–5.34) in a longitudinal cohort study of children.^[46] Recent studies highlight a dose-response where high early exposure may promote tolerance via modified Th2 responses and IgG4 production.^[47]

Distribution and Homologs

Environmental Spread

Fel d 1, the primary cat allergen, disperses into human environments primarily through airborne transmission, attaching to dander particles ranging from less than 1 to over 20 μm in diameter. These particles, generated from shed skin and fur coated with salivary secretions, can remain suspended in indoor air for several hours, facilitating inhalation and subsequent deposition on surfaces such as furniture and flooring. Approximately 60% of airborne Fel d 1 is carried on such small particles, with 75% exceeding 5 μm and 25% below 2.5 μm, enhancing its ability to penetrate deep into the respiratory tract.^[30]^[48]^[49] The allergen exhibits remarkable persistence in the environment, remaining stable on fabrics and upholstery for months due to its resistance to degradation. This longevity allows Fel d 1 to accumulate in reservoirs like carpets, mattresses, and soft furnishings, where it can be resuspended into the air through human activity. Consequently, it has been detected in the settled dust of 95% of homes without cats (38 out of 40 surveyed), primarily through indirect transfer via owners' clothing, hair, or visitors, underscoring its ubiquity even in pet-free settings.^[50] Quantification of Fel d 1 in environmental samples relies on sensitive methods such as enzyme-linked immunosorbent assay (ELISA) for dust swabs, which detect levels as low as 0.1 ng/g, and air samplers that measure concentrations in the range of ng/m³ to μg/m³. These techniques enable assessment of exposure risks in homes and public spaces, with airborne levels in cat-owning households typically ranging from 0.7 to 38 ng/m³.^[49] Key factors influencing Fel d 1 dissemination include grooming behaviors, during which salivary secretions containing the allergen are spread onto the fur and subsequently aerosolized, and environmental controls like ventilation, which can significantly reduce airborne concentrations through dilution and particle removal. Regular bathing of cats further mitigates spread by temporarily lowering salivary and airborne Fel d 1 by up to 79%.^[51]

Presence in Other Species

Fel d 1 exhibits high sequence conservation across the Felidae family, with protein sequence identities ranging from 80% to 98% between domestic cats and exotic felids such as lions and tigers.^[15] Specifically, chain 1 shows approximately 90.4% identity on average among exotic felids, while chain 2 averages 86.9%, reflecting evolutionary divergence within the family but retaining core structural features.^[15] This protein is expressed similarly in the salivary glands of these species, contributing to its secretion via grooming behaviors analogous to those in domestic cats.^[15] Homologous sequences to Fel d 1 have been identified in other mammals outside the Felidae family, displaying 25-50% sequence similarity to proteins like rabbit uteroglobin and subunits of rat prostatein, both members of the secretoglobin superfamily.^[15] However, no functional equivalents of Fel d 1 are expressed in non-felid species such as dogs or humans, limiting its presence to the Felidae lineage.^[47] Bioinformatics analyses have detected Fel d 1 orthologs in 37 exotic felid species spanning eight evolutionary lineages, underscoring its broad distribution within the family.^[15] Evidence of positive selection on epitopes, particularly in chain 2 (observed in 95% of exotic felids), suggests adaptive evolution that may influence immune recognition while preserving overall function.^[15] Fel d 1 from wild felids demonstrates significant cross-reactivity with human IgE antibodies specific to domestic cat Fel d 1, with studies showing high cross-reactivity, including 100% in a small cohort of cat-allergic individuals exposed in zoo environments.^[52] This cross-reactivity extends to species like lions, tigers, pumas, and jaguars, posing risks for allergic reactions during encounters with big cats in captivity.^[53]

Recent Research and Mitigation

Gene Editing Approaches

Gene editing approaches for Fel d 1 primarily utilize CRISPR-Cas9 to target and disrupt the genes encoding its chains, aiming to produce hypoallergenic cats by reducing or eliminating allergen secretion. In a 2025 study, researchers achieved a 40% knockout efficiency for the CH2 gene in cat fetal fibroblasts using CRISPR-Cas9 with two sgRNAs, resulting in mutations that eliminated key antigenic sites and reduced allergenicity through frameshifts.^[54] This in vitro success laid groundwork for subsequent applications, demonstrating the feasibility of editing without significant off-target effects. Building on this, a 2024 study generated the first live CH2 genome-edited cats via CRISPR-Cas9 microinjection into zygotes, followed by cloning through somatic cell nuclear transfer. Homozygous edited kittens exhibited normal development and viability, with no observed health abnormalities up to several months post-birth. Fel d 1 levels in their saliva and fur were drastically reduced, reaching less than 1% of wild-type levels (e.g., 0.15 µg/ml in saliva versus 10.69 µg/ml in controls), confirming substantial allergen suppression.^[4] Editing the CH1 chain presents greater challenges due to its higher conservation and fewer polymorphic sites compared to CH2, leading to lower targeting success amid multiple alleles. Biallelic edits in CH2 models achieved over 98% reduction in expression, but dual CH1/CH2 targeting remains technically demanding and requires further optimization for complete knockout.^[4]^[54] Ethical considerations include ensuring animal welfare, as Fel d 1's biological role in cats is not fully understood, potentially affecting reproduction or immunity if disrupted. Commercially, these advances hold promise for developing hypoallergenic breed lines to meet demand from allergy sufferers, but face regulatory hurdles; in the US, the FDA classifies intentionally genome-edited animals as new animal drugs, requiring rigorous safety reviews for human, animal, and environmental risks before market approval.^[55]^[56]

Neutralization Methods

Neutralization methods for Fel d 1 focus on strategies that target the allergen post-production, either by binding it in the cat's system or reducing its environmental presence to limit human exposure. These approaches aim to inactivate or block Fel d 1 without altering the cat's genetic expression of the protein. Key techniques include dietary interventions using antibodies, vaccines administered to cats, allergen-specific immunotherapy for humans, and environmental controls. One prominent antibody-based method involves incorporating chicken-derived IgY antibodies specific to Fel d 1 into cat food, such as the Purina Pro Plan LiveClear formula introduced in 2019. These antibodies bind to Fel d 1 in the cat's digestive tract, facilitating its excretion via feces and thereby reducing the amount of active allergen secreted in saliva and subsequently transferred to fur during grooming. A clinical study demonstrated that feeding this diet to cats resulted in a 47% reduction in active Fel d 1 levels on their hair after three weeks, with effects persisting over longer periods of use.^[57] This approach is non-invasive and safe for cats, offering a practical way for pet owners to mitigate allergen spread in the household. Vaccine development represents another strategy, where cats are immunized to produce their own neutralizing antibodies against Fel d 1. The HypoCat vaccine, tested in trials during the 2000s and 2010s, utilized a recombinant Fel d 1 antigen conjugated to a virus-like particle to induce high-titer IgG antibodies in cats that bind and neutralize the allergen in bodily secretions. Studies involving over 70 cats showed that vaccination led to a reduction of up to 60% in active Fel d 1 levels, correlating with decreased allergic symptoms in exposed humans. Although the HypoCat program was discontinued, its findings have provided foundational insights for subsequent vaccine designs targeting feline allergens.^[58] For human patients, allergen-specific immunotherapy (AIT) using extracts from cat dander offers a direct approach by gradually desensitizing the immune system to allergens including Fel d 1. Clinical trials of sublingual administration have demonstrated improvements in symptoms for cat-allergic individuals.^[59] Recent developments also include monoclonal antibody therapies, such as the combination REGN1908 and REGN1909, which target Fel d 1 and have shown reductions in early asthmatic responses and rhinitis symptoms in phase 1/2 trials conducted in 2022.^[60] Household interventions provide indirect neutralization by physically removing or trapping Fel d 1 from the air and surfaces. High-efficiency particulate air (HEPA) filters in air purifiers and HVAC systems capture airborne Fel d 1 particles, while regular cat washing and home cleaning further diminish allergen reservoirs. Seminal studies have shown that combining HEPA filtration with cat bathing can reduce airborne Fel d 1 concentrations by approximately 80%, significantly lowering exposure for allergic residents.^[61] These non-pharmacological measures are accessible and effective as first-line defenses, particularly in multi-pet homes.

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Fel d 1 and Can f 1 have been measured in reservoir dust from seats and floors inside public buildings such as hotels, cinemas and pubs (74), hospitals (69), ...Missing: transmission | Show results with:transmission
[43]
Distribution, aerodynamic characteristics, and removal of the major ...
Airborne levels of Fel d 1 were detected in all houses with cats, and the levels varied greatly between the homes (range 0.7-38 ng/m3). Low concentrations of ...
[44]
Minimizing indoor allergen exposure: What works? - PMC - NIH
Fel d 1 is a “persistent” allergen, and it may take months for the allergen load to be reduced once a cat is removed from the household. One study observed ...<|separator|>
[45]
Cat antigen in homes with and without cats may induce ... - PubMed
Fel d 1 was present in the settled dust of 38 of 40 homes without cats (range, 39 to 3750 ng/gm; median, 258 ng/gm), although these levels were only weakly ...Missing: detection percentage transfer clothing<|separator|>
[46]
Human allergy to cats: A review for veterinarians on prevalence ...
Oct 8, 2021 · Increasing ventilation will help to reduce airborne Fel d 1 concentrations ... One study demonstrated a mean reduction of 79% in airborne Fel d 1 ...
[47]
Anti-Fel d1 immunoglobulin Y antibody-containing egg ingredient ...
Jul 16, 2019 · Fel d1 is the major cat allergen, causing IgE reactions in up to 90% of cat-allergic adults. Fel d1 secreted in saliva is spread to the haircoat ...
[48]
Evolutionary Biology and Gene Editing of Cat Allergen, Fel d 1
Mar 28, 2022 · Fel d 1 causes IgE antibody-mediated sensitization in ∼95% of cat allergic patients and accounts for 60–90% of the anti-cat IgE. High ...<|control11|><|separator|>
[49]
Evidence for a Fel d I-like molecule in the "big cats" (Felidae species)
In this study, we investigated the cross-reactivity pattern of IgE and IgG4 antibodies to the major feline allergen, Fel d I. We studied the IgE and IgG4 ...Missing: zoo | Show results with:zoo
[50]
Molecular diagnosis in cat allergy - PMC - PubMed Central
May 20, 2021 · The benefits of molecular diagnosis in cat allergy include use of the species-specific major allergen Fel d 1, cross-reacting allergen components.Missing: 1988 | Show results with:1988
[51]
Targeted Gene Knock-Out of Fel d1 in Fetal Fibroblasts Using ...
There are 2 SNP sites in CH1 exon 2, and the CH2 sequence has a total of 31 SNP sites in other regions. In addition, it was also found that the CH1 sequence in ...Missing: chromosome | Show results with:chromosome
[52]
Genetic engineering of animals: Ethical issues, including welfare ...
The genetic engineering of animals has increased significantly in recent years, and the use of this technology brings with it ethical issues, some of which ...Missing: hurdles | Show results with:hurdles
[53]
Are cats drugs? That's how outdated FDA regulations categorize ...
Apr 27, 2022 · A controversial company called Lifestyle Pets (formerly Allerca) claimed to have produced hypoallergenic cats using conventional breeding.Missing: hurdles | Show results with:hurdles