Recombinant Olea europaea Pollen allergen Ole e 7, partial

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Description

Clinical and Immunological Significance

Ole e 7 sensitization is linked to severe allergic phenotypes, particularly in regions with high olive pollen exposure . Key findings include:

  • Prevalence: 14.4%–60% among olive pollen-allergic patients, depending on geographic pollen levels .

  • Cross-Reactivity: Clinically relevant cross-reactivity with food nsLTPs (e.g., Pru p 3 in peach) due to structural homology .

  • Disease Associations:

    • Asthma and severe rhinoconjunctivitis in olive pollinosis .

    • Anaphylaxis to Rosaceae (peach) and Cucurbitaceae (melon) fruits .

Table 2: Clinical Associations of Ole e 7 Sensitization

Clinical FeatureStudy Population (%)Key Reference
Asthma24.1 (adults)
Fruit Anaphylaxis47.9
Polysensitization (≥3 allergens)75

Component-Resolved Diagnostics (CRD)

Recombinant Ole e 7, partial, is used to:

  • Identify patients with nsLTP-driven cross-reactive allergies .

  • Differentiate between mild (oral allergy syndrome) and severe (anaphylaxis) food allergy phenotypes .

Table 3: IgE Reactivity in Olive Pollen-Allergic Patients

AllergenIgE Positivity (%)Clinical Correlation
Ole e 170–80Mild respiratory symptoms
Ole e 735–60Severe asthma, food anaphylaxis
Ole e 950High pollen exposure regions

Therapeutic Potential

  • Immunotherapy: Not yet clinically available, but recombinant Ole e 7’s stability and IgE-binding capacity make it a candidate for hypoallergenic vaccines .

  • Research Use: Facilitates studies on nsLTP cross-reactivity mechanisms and epitope mapping .

Production and Validation

  • Proteomic Assembly: The natural Ole e 7 sequence was inferred via de novo mass spectrometry after tryptic digestion and LC-MS/MS analysis .

  • Validation: Circular dichroism and immunoassays confirmed structural/functional equivalence to natural Ole e 7 .

  • Purity: >85% by SDS-PAGE, with endotoxin levels suitable for in vitro assays .

Limitations and Future Directions

  • Partial Sequence: The 21-amino-acid fragment may not capture full conformational epitopes .

  • Geographic Variability: Diagnostic utility is highest in Mediterranean regions with intense olive cultivation .

  • Therapeutic Gaps: Recombinant Ole e 9 and other olive pollen allergens remain challenging to produce .

Product Specs

Form
Lyophilized powder. We will ship the available format, but please specify any format requirements when ordering.
Lead Time
Delivery times vary by purchase method and location. Consult your local distributor for specific delivery times. Proteins are shipped with blue ice packs by default. Request dry ice in advance for an extra fee.
Notes
Avoid repeated freeze-thaw cycles. Working aliquots are stable at 4°C for up to one week.
Reconstitution
Briefly centrifuge the vial before opening. Reconstitute in sterile deionized water to 0.1-1.0 mg/mL. Add 5-50% glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final glycerol concentration is 50%.
Shelf Life
Shelf life depends on storage conditions, buffer components, storage temperature, and protein stability. Liquid form is generally stable for 6 months at -20°C/-80°C. Lyophilized form is generally stable for 12 months at -20°C/-80°C.
Storage Condition
Store at -20°C/-80°C upon receipt. Aliquot for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
The tag type is determined during manufacturing. If you require a specific tag, please inform us and we will prioritize its development.
Synonyms
Pollen allergen Ole e 7; Allergen Ole e VII; allergen Ole e 7; Fragment
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
1-21
Protein Length
Partial
Purity
>85% (SDS-PAGE)
Species
Olea europaea (Common olive)
Target Protein Sequence
APSQSTVTAL LTSCVSYIDD Q
Uniprot No.

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