Recombinant Legumin protein (His tag) is a Fava Bean Fragment protein, in the 1 to 148 aa range, expressed in Yeast, with >90% purity and suitable for SDS-PAGE.
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
This protein found in the seeds of many leguminous and non-leguminous plants is the source of sulfur-containing amino acids in seed meals.
Legumin type B, LEB6
Recombinant Legumin protein (His tag) is a Fava Bean Fragment protein, in the 1 to 148 aa range, expressed in Yeast, with >90% purity and suitable for SDS-PAGE.
pH: 7.2 - 7.4
Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
This protein found in the seeds of many leguminous and non-leguminous plants is the source of sulfur-containing amino acids in seed meals.
Belongs to the 11S seed storage protein (globulins) family.
Legumin also known as Vicilin is a protein with a molecular mass of approximately 300 kDa. This protein is mainly found in seeds and is a major storage protein in legumes like peas and lentils. It plays an essential role in providing amino acids during seed germination supplying the necessary building blocks for young plant development. The existence of Legumin with its multiple subunits allows it to store high amounts of protein within the seed structure facilitating nutrient availability when the seed begins to grow.
Legumin functions as a storage protein and supports the early stages of plant growth. It forms part of the seed storage protein complex and assists in nutrient provision during germination. This complex nature enables the plant to have a stable reserve of proteins that decompose into amino acids needed for plant metabolism and development. Legumin also exhibits strong allergenic properties in some individuals as it contains specific allergenic epitopes that can trigger immune responses.
Legumin acts in the context of nitrogen and sulfur assimilation pathways in plants. These pathways are important for amino acid and protein synthesis in seeds. Related proteins such as glutelin and glycinin also contribute to these pathways by breaking down into smaller peptides that influence cellular processes. During seed germination Legumin interacts within the storage protein degradation pathway contributing to the mobilization of nutrients that enable seedling growth.
Legumin has a close association with food allergies in humans such as pea allergy. The allergenic properties stem from specific protein structures that initiate hypersensitivity reactions in individuals. Legumin shares similarities with other allergenic proteins such as Ara h 1 found in peanuts which can lead to cross-reactivity and further complicate allergic responses in sensitive individuals. Understanding these interactions helps in the development of allergen-reduced legume varieties aiming to minimize adverse health impacts.
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(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) analysis with 5% enrichment gel and 15% separation gel of ab240848.
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