Date allergens, particularly the notorious Ziz m 1, have become a focal point in allergy research, unraveling the complexities of molecular interactions that trigger allergic reactions. These allergens are proteins found in dates and belong to the molecular family of storage proteins.
Date allergen proteins are primarily composed of Ziz m 1, a major allergen identified in dates. Ziz m 1 belongs to the family of storage proteins, which play a crucial role in storing nutrients for the plant. These proteins are characterized by their unique structures, often formed by intricate folding patterns that give them specific functions.
Ziz m 1, like many allergen proteins, exhibits a complex structure. Its classification is based on its specific molecular features and its ability to induce allergic reactions. Understanding the structural intricacies of Ziz m 1 is vital in comprehending its allergenic properties.
| Cat.No. | Product Name | Species | Source | Tag |
| ra-3846P | Recombinant Ziz m 1 | Ziziphus mauritiana (Chinese-date) | E.coli or Yeast | His |
Date allergens, particularly Ziz m 1, play a central role in triggering allergic responses in susceptible individuals. The molecular mechanisms behind these allergic reactions involve the interaction between the allergen proteins and the immune system. Sensitization to Ziz m 1 can lead to the production of specific antibodies, setting the stage for allergic reactions upon subsequent exposure to dates.
The molecular mechanisms that cause allergy involve a cascade of events initiated by the interaction between Ziz m 1 and the immune system. Upon exposure, the allergen is recognized by immune cells, leading to the release of inflammatory mediators. This immune response manifests as allergic symptoms, ranging from mild discomfort to severe anaphylaxis.
Beyond the realm of allergy research, Date allergen proteins find intriguing applications in various biomedical fields, opening avenues for diagnostic development, vaccine formulation, and treatment strategies.
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