Seed storage protein. Highly thermostable. Loss of stability only after incubation for 1 hour at 100 degrees Celsius. Homohexamer. Expressed in seeds (at protein level). Expressed in immature seeds at 20 days after flowering (PubMed:18980324). Expressed in radicles (PubMed:16717422). Proteolytically processed from a single precursor to produce an acidic and a basic chain that are linked by a disulfide bond. Causes an allergic reaction in human (PubMed:18980324, PubMed:16717422, PubMed:15277744, PubMed:20431913, PubMed:21571740, PubMed:22449541). Natural protein binds to IgE in all 5 buckwheat-allergic patients tested. Natural protein is susceptible to digestion with pepsin, but resistant to digestion with trypsin. Recombinant protein binds to IgG of buckwheat-allergic patients (PubMed:22449541). Recombinant full-length protein (rTBt) binds to IgE of patients allergic to buckwheat (PubMed:18980324, PubMed:22449541). Recombinant N-terminal subunit (rTBb) binds to IgE of patients allergic to buckwheat (PubMed:21571740). Recombinant C-terminal subunit (rTBa) binds to IgE of patients allergic to buckwheat (PubMed:18980324, PubMed:16717422, PubMed:20431913). Natural 24 kDa protein binds to IgE of patients allergic to buckwheat (PubMed:15277744). Both the recombinant rTBb and rTBa have higher IgE-binding activity than rTBt (PubMed:18980324). This protein, when mutated, can potentially be applicable to the development of transgenic hypoallergenic crops of tartarian buckwheat and specific immunotherapy to treat tartarian buckwheat allergy (PubMed:20431913, PubMed:21571740). Destructing the native conformation of this protein significantly reduces its allergenicity and it may be a candidate for the development of vaccine that builds immunotolerance in individuals with buckwheat allergy. Production of mosaic molecules which are reassembled derivatives of the protein may have advantages compared to production of modified fragments. The treatment can be achieved with a single molecule that is more stable and easier to produce and purify. The production is also more cost-effective than with chemically modified allergens (PubMed:22449541). Belongs to the 11S seed storage protein (globulins) family.