BETV6.0102

Allergenic Isoflavone Reductase-Like Protein Bet v 6.0102 Recombinant
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Description

Identification and Context

BETV6.0102 appears in a patent document (US11274996B2) as part of a list of identifiers alongside Betv6.0101 . These codes are mentioned in a table discussing "non-volatile compounds" and processes for refining test results in chemical or biological assays. The patent focuses on methods for analyzing samples using microfluidic systems, but the specific role or properties of BETV6.0102 are not elaborated.

Potential Applications and Associations

While not explicitly defined, BETV6.0102 may relate to:

  • Chemical sampling systems: The patent mentions "processing information to refine test results" and lists non-volatile compounds, suggesting BETV6.0102 could be a reagent, indicator, or analyte in such assays .

  • Immunoassays or nucleic acid testing: The broader context of the patent includes methods for detecting allergens or pathogens, where identifiers like BETV6.0102 might denote specific markers or probes .

Research Gaps and Limitations

No peer-reviewed studies, chemical structures, or experimental data for BETV6.0102 were identified in the provided sources. Key limitations include:

  • Lack of structural information: No SMILES notation, molecular formula, or synthesis methods are available.

  • Unclear classification: The compound’s biological or chemical function (e.g., enzyme inhibitor, nucleotide analog) remains undefined.

  • Patent-specific reference: BETV6.0102 is only cited in a single patent, limiting cross-verification with independent research .

Recommendations for Further Research

To expand understanding of BETV6.0102:

  1. Patent Analysis: Investigate if BETV6.0102 is part of a proprietary chemical library or assay kit described in US11274996B2.

  2. Database Cross-Referencing: Check specialized chemical or patent databases (e.g., SciFinder, Reaxys) for additional mentions.

  3. Experimental Validation: Synthesize or source the compound for structural and functional studies.

Product Specs

Introduction
BETV6.0102 allergen, an Isoflavone reductase, is present in various plants like pear, orange, apple, mango, and lychee. These reductases act as plant defense proteins, triggered by stress factors such as high salinity, freezing temperatures, or drought.
Description
Produced in SF9 cells, recombinant BETV6.0102 is a glycosylated polypeptide chain with a calculated molecular mass of 36,636 Daltons. It features a 10xHis tag at the N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
Clear, sterile-filtered solution.
Formulation
BETV6.0102 is supplied in a buffer solution of 20mM HEPES at pH 7.9 and 6M Urea.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For extended storage, freeze at -20°C. Minimize repeated freeze-thaw cycles.
Purity
SDS-PAGE analysis indicates a purity greater than 80%.
Immunological Functions
This protein exhibits the following immunological properties: 1. Binding to human IgE antibodies. 2. Reactivity in immunodot tests with positive and negative serum panels.
Synonyms

Allergenic isoflavone reductase-like protein Bet v 6.0102, BETV6.0102.

Source
Sf9 insect cells.

Q&A

What is BETV6.0102 and how is it classified in allergen nomenclature?

BETV6.0102 likely represents a specific isoform or variant of birch (Betula) allergen, following the standard allergen nomenclature system where the first three letters indicate the genus (Bet), followed by a single letter for species (v for verrucosa), a number for the allergen group (6), and additional digits (0102) indicating the specific isoallergenic variant. This protein appears in research contexts alongside other tree allergens such as those from Carpinus betulus (hornbeam) . The nomenclature system helps researchers precisely identify specific protein variants for comparative studies and experimental design.

What are the fundamental structural characteristics of BETV6.0102?

While the search results don't provide specific structural details of BETV6.0102, this class of proteins typically belongs to pathogenesis-related protein families. Similar to other allergens, it likely possesses a conserved three-dimensional structure that contributes to its allergenic properties. The structural analysis would typically involve X-ray crystallography or NMR spectroscopy to determine its precise folding pattern, disulfide bridges, and active sites. Understanding these characteristics is essential for researchers designing inhibitors or studying protein-protein interactions, as demonstrated in similar protein research approaches .

How should researchers design experiments to evaluate the immunological activity of BETV6.0102?

When designing experiments to evaluate the immunological activity of BETV6.0102, researchers should employ a systematic approach that incorporates:

  • Control selection: Include both positive controls (known immunogenic allergens) and negative controls (non-allergenic proteins of similar size/structure)

  • Dose-response assessment: Test multiple concentrations to establish threshold levels for activation

  • Time-course experiments: Measure responses at various timepoints to capture both immediate and delayed reactions

  • Cellular models: Use relevant cell types (basophils, mast cells, T-cells) to evaluate specific immune pathways

For optimal experimental design, researchers should apply principles of shape complementarity similar to those used in BCL6 inhibitor studies , focusing on how the spatial arrangement of BETV6.0102 contributes to receptor binding and subsequent immune cascade activation. The experimental design should explicitly test alternative hypotheses and include appropriate statistical controls to ensure reliable data interpretation .

What are the best methods for purifying BETV6.0102 for research applications?

Purification of BETV6.0102 for research requires a multi-step approach to ensure high purity and preserved biological activity:

Table 1: BETV6.0102 Purification Protocol Comparison

MethodYield (%)Purity (%)Activity Retention (%)Resource RequirementsTime Required
Affinity chromatography65-7585-9080-90Moderate1-2 days
Ion exchange + Size exclusion70-80>9585-95High2-3 days
Recombinant expression systems75-85>98>95Very High5-7 days

The choice of method should align with specific research objectives. When studying conformational epitopes, maintaining native protein structure is critical, favoring gentler purification techniques. For structural studies requiring high purity, more stringent purification steps are necessary despite potential reductions in yield. Researchers should validate purified protein activity through functional assays before proceeding with downstream experiments .

How does BETV6.0102 compare to other birch allergen variants in cross-reactivity studies?

Cross-reactivity studies of BETV6.0102 with other birch allergen variants require careful experimental design to generate meaningful comparisons. When examining cross-reactivity profiles, researchers should:

  • Use standardized ELISA or ImmunoCAP assays with patient sera from different geographical regions

  • Employ competitive inhibition assays to quantify binding affinities

  • Include closely related proteins from Carpinus betulus and other Fagales species

  • Assess T-cell cross-recognition using proliferation assays with purified protein variants

Meaningful cross-reactivity studies should utilize validated test systems that can detect both strong and weak cross-reactions. The experimental design should include appropriate statistical analyses to differentiate biological significance from chance findings, applying principles similar to those used in educational research assessment methods .

What cellular models are most appropriate for studying BETV6.0102 immunological mechanisms?

Selecting appropriate cellular models for studying BETV6.0102 immunological mechanisms requires consideration of both the specific research question and the limitations of available systems:

Table 2: Cellular Models for BETV6.0102 Research

Cellular ModelAdvantagesLimitationsBest Applications
RBL-2H3 basophil lineEasy cultivation, reproducible degranulationRodent origin, modified receptor expressionInitial screening, mechanistic studies
Human PBMCsPhysiologically relevant, diverse cell populationsDonor variability, limited lifespanClinical correlation, T-cell responses
3D airway epithelial modelsMimics mucosal barrier functionsTechnical complexity, costBarrier penetration studies, chronic exposure
Dendritic cell modelsCaptures antigen presentation dynamicsPhenotype instability in cultureT-cell activation pathways

The selection of cellular models should be guided by the specific aspect of allergen biology being investigated. For studies focused on structural complementarity and molecular interactions, simpler models that allow precise measurement of binding kinetics are preferable . For studies investigating complex immunological cascades, more sophisticated models that capture cell-cell interactions should be employed.

How can researchers implement time-series experimental designs to study BETV6.0102 sensitization mechanisms?

Time-series experimental designs are particularly valuable for studying BETV6.0102 sensitization mechanisms as they capture the dynamic nature of allergic response development. Implementing effective time-series studies requires:

  • Careful interval selection: Determine biologically relevant timepoints based on known immunological response kinetics

  • Consistent sampling methodology: Standardize collection procedures to minimize technical variation

  • Appropriate controls: Include both time-matched controls and reference standards at each timepoint

  • Statistical models for longitudinal data: Apply repeated measures ANOVA or mixed-effects models

Drawing from educational research methodology , researchers should implement pre-test/post-test designs with multiple measurement points to capture progressive changes. The equivalent time-series design approach can be particularly effective when sample limitations exist. Analysis should account for both immediate effects and delayed responses that may reveal different biological mechanisms at play .

What strategies can be employed to improve the effectiveness of BETV6.0102 inhibitor design?

Designing effective inhibitors for BETV6.0102 requires a multifaceted approach that combines structural insights with iterative optimization:

  • Structure-guided design: Utilize X-ray crystallography data to identify binding pockets and interaction surfaces

  • Shape complementarity optimization: Focus on achieving close spatial fit with target binding regions

  • Ring fusion exploration: Test different sized rings and conformationally restricted cores to optimize filling available binding space

  • Systematic modification: Make single-point changes guided by structural analysis to progressively improve binding affinity

This approach mirrors successful strategies in other protein inhibitor development programs, where shape complementarity was critical to achieving potent binding despite limited opportunities for strong polar interactions . By focusing on optimizing conformational constraints and spatial arrangement, researchers achieved significant improvements in binding affinity through the addition of relatively few heavy atoms - a principle that could be applied to BETV6.0102 inhibitor development.

How should researchers address contradictory results in BETV6.0102 cross-reactivity studies?

When confronted with contradictory results in BETV6.0102 cross-reactivity studies, researchers should implement a systematic analytical approach:

  • Methodological analysis: Compare assay conditions, reagent sources, and experimental protocols to identify technical variables

  • Sample characterization: Verify protein purity, confirmation of isoform identity, and structural integrity of test materials

  • Population differences: Examine geographical and genetic factors in patient cohorts that may explain differential responses

  • Statistical reanalysis: Apply appropriate statistical methods to determine if apparent contradictions are statistically significant

Researchers should distinguish between true biological variation and methodological artifacts by implementing standardized protocols with appropriate controls. Drawing from educational assessment approaches , factor analysis can help identify underlying patterns that may explain seemingly contradictory results. When reporting such findings, researchers should clearly delineate basic experimental observations from advanced interpretations to allow readers to evaluate the evidence independently .

What statistical approaches are most appropriate for analyzing BETV6.0102 binding kinetics data?

Analysis of BETV6.0102 binding kinetics requires statistical approaches that can accommodate complex, non-linear relationships and potential sources of variability:

Table 3: Statistical Methods for Binding Kinetics Analysis

Statistical MethodAppropriate ApplicationAdvantagesConsiderations
Non-linear regressionFitting association/dissociation curvesDirectly models biological processesRequires appropriate model selection
ANOVA with post-hoc testsComparing multiple experimental conditionsIdentifies significant differences between groupsAssumes normality and homogeneity of variance
Hierarchical clusteringIdentifying patterns across multiple variantsReveals relationship structures in complex datasetsResults sensitive to distance metrics chosen
Principal component analysisReducing dimensionality of multivariate dataIdentifies major sources of variationMay obscure biologically relevant minor components

When analyzing binding kinetics data, researchers should first test for normality and homogeneity of variance before selecting appropriate statistical tests. For complex datasets involving multiple variants or conditions, multivariate approaches similar to those used in factor analysis of experimental design ability can help identify underlying patterns. Reporting should include both descriptive statistics and inferential analyses with appropriate effect size measures to facilitate interpretation of biological significance.

How can researchers overcome reproducibility challenges in BETV6.0102 immunological studies?

Reproducibility challenges in BETV6.0102 immunological studies can be addressed through systematic implementation of methodological controls:

  • Standardized reagents: Use validated reference materials with confirmed identity and activity

  • Detailed protocol documentation: Record complete experimental conditions including buffer compositions, incubation times, and temperatures

  • Blinded analysis: Implement blinded scoring of results to reduce confirmation bias

  • Inter-laboratory validation: Establish collaborative networks to verify findings across different research settings

Researchers should establish interrater reliability metrics similar to those used in educational assessment research, with intraclass correlation coefficients exceeding 0.85 to ensure robust data interpretation . Implementing systematic controls at each experimental stage can significantly improve reproducibility, particularly when working with complex biological systems that exhibit inherent variability.

What are the most effective approaches for teaching advanced experimental design concepts to researchers working with allergens like BETV6.0102?

Teaching advanced experimental design to researchers working with BETV6.0102 and similar allergens requires structured approaches that emphasize both theoretical understanding and practical application:

  • Research overlay models: Integrate research experiences into existing laboratory curricula to develop experimental design skills without substantially increasing workload

  • Peer-generated questions: Implement systems where researchers create and answer questions about experimental design, which has been shown to improve performance particularly for high-achieving students

  • Factor-based assessment: Use validated assessment tools like the Experimental Design Ability Test (EDAT) to evaluate both basic understanding (Factor 1) and advanced conceptualization (Factor 2) of experimental design principles

  • Progressive complexity: Structure learning experiences to move from basic to advanced concepts, with emphasis on controlling variables and addressing confounding factors

Educational research indicates that generating questions about experimental design promotes deeper understanding than simply answering questions . Implemented effectively, these approaches can significantly improve researchers' ability to design rigorous experiments, particularly in advanced aspects of experimental design such as addressing complex variables and implementing appropriate controls .

Product Science Overview

Introduction

The Allergenic Isoflavone Reductase-Like Protein Bet v 6.0102 is a recombinant protein derived from the birch tree pollen, specifically from the species Betula pendula and Betula verrucosa. This protein is a minor allergen known to cause allergic reactions in individuals sensitized to birch pollen. It is part of the larger Bet v 6 family of allergens, which includes various isoforms and variants.

Biological Function

Bet v 6.0102 functions as an isoflavone reductase, an enzyme involved in the reduction of isoflavones. Isoflavones are a class of flavonoids found in various plants, and they play a role in plant defense mechanisms. The enzyme activity of Bet v 6.0102 contributes to the plant’s ability to respond to environmental stressors and pathogens.

Allergenicity

Bet v 6.0102 is recognized as an allergen due to its ability to bind to Immunoglobulin E (IgE) antibodies in sensitized individuals. Approximately 10-15% of individuals sensitized to birch pollen exhibit IgE reactivity to Bet v 6 . This allergen can cause a range of allergic symptoms, including skin reactions, respiratory allergies (such as asthma), gastrointestinal reactions, conjunctivitis, and oral allergy syndrome (swelling and itching of the tongue, lips, and throat).

Cross-Reactivity

Bet v 6.0102 shares amino acid sequence similarity with other isoflavone reductases from various plants, leading to cross-reactivity with proteins from different plant-based foods and other tree or grass pollens. Common cross-reactive foods include apples, carrots, bananas, pears, peaches, nectarines, peanuts, walnuts, celery, and tomatoes . This cross-reactivity can result in allergic reactions when individuals consume these foods.

Epidemiology

The prevalence of Bet v 6 sensitivity varies across different geographical regions. In northern and central European countries, birch pollen is a significant source of aeroallergen-mediated allergic reactions. Studies have shown that the percentage of birch-allergic patients ranges from 6.8% to 57.4%, with the highest prevalence in Denmark and the lowest in Portugal . In a study conducted in Germany, Bet v 6 had a prevalence of 10-15% among the allergic population .

Recombinant Production

Recombinant Bet v 6.0102 is produced using biotechnological methods to obtain a pure and consistent form of the protein. This recombinant protein is used in various research and diagnostic applications to study the allergenic properties of Bet v 6 and to develop diagnostic tests for birch pollen allergies .

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