Legumin Antibody (1H9) is a mouse monoclonal IgG1 antibody that detects Legumin protein of Faba bona, Pisum sativum, Lens culinaris, Vicia cracca, and Melilotus albus by enzyme-linked immunosorbent assay (ELISA). Anti-Legumin antibody (1H9) plays a crucial role in studying leguminous plants, as Legumin is a primary storage protein found in pea seed vacuoles, serving as a vital source of sulfur-containing amino acids essential for nutrition. Legumin′s structure consists of multiple polypeptides that form mixed hexamers through post-translational cleavage, allowing for diverse functional properties. Such structural versatility enhances stability and facilitates aggregation into nanoparticles, which can be chemically cross-linked with agents like glutaraldehyde. Legumin regulation remains tightly controlled during development and responds to environmental changes, making Legumin a key player in plant adaptation and growth. Studying Legumin′s dynamics and interactions provides insights into plant biology and improves agricultural practices, particularly in legume cultivation.
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.
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Legumin Antibody (1H9) References:
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- Two cDNA clones coding for the legumin protein of Pisum sativum L. contain sequence repeats. | Lycett, GW., et al. 1984. Plant Mol Biol. 3: 91-6. PMID: 24310304
- Two genes encoding 'minor' legumin polypeptides in pea (Pisum sativum L.). Characterization and complete sequence of the LegJ gene. | Gatehouse, JA., et al. 1988. Biochem J. 250: 15-24. PMID: 3355508
- Isolation and characterization of a minor legumin and its constituent polypeptides from Pisum sativum (pea). | March, JF., et al. 1988. Biochem J. 250: 911-5. PMID: 3390145
- Comparative structural and emulsifying properties of ultrasound-treated pea (Pisum sativum L.) protein isolate and the legumin and vicilin fractions. | Sha, L. and Xiong, YL. 2022. Food Res Int. 156: 111179. PMID: 35651040
- Structural properties of pea proteins (Pisum sativum) for sustainable food matrices. | Grossmann, L. 2024. Crit Rev Food Sci Nutr. 64: 8346-8366. PMID: 37074167
- Unraveling distinct potential of pea (Pisum sativum L.) fractions (legumin, vicilin and albumin) by structural and functional characterization. | Tahir, AB., et al. 2024. Food Res Int. 198: 115332. PMID: 39643340
- Isoelectric-focusing properties and carbohydrate content of pea (Pisum sativum) legumin. | Gatehouse, JA., et al. 1980. Biochem J. 185: 497-503. PMID: 7396828