S9896
Saporin Peptide
lyophilized powder, from Saponaria officinalis seeds
Synonyme(s) :
Saponin Extract
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About This Item
Produits recommandés
Nom du produit
Saporin from Saponaria officinalis seeds, lyophilized powder
Source biologique
plant seeds (Saponaria officinalis)
Niveau de qualité
Essai
10.00-30.00%
Forme
lyophilized powder
Composition
Protein, ~20% Lowry
Technique(s)
activity assay: suitable
Température de stockage
2-8°C
Description générale
Saporin from Saponaria officinalis seeds has an N-terminal domain which is β-stranded and a C-terminal domain which is α-helical. It is made up of 253 amino acids and has a molecular weight of 28,621Da.
Application
Saporin from Saponaria officinalis seeds has been used to study its antifungal activity against Fusarium verticillioides.
Actions biochimiques/physiologiques
Saporin from Saponaria officinalis seeds is a ribosome inactivating protein. It is used for the preparation of immunoconjugates. It has been shown to induce the formation of micronuclei in cultured human lymphocytes, thereby reducing cell viability and enhancing apoptosis.
Conditionnement
Package size based on protein content.
Forme physique
Lyophilized powder containing glucose and sodium phosphate buffer salts
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
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The crystal structure of saporin SO6 from Saponaria officinalis and its interaction with the ribosome.
Savino C
Febs Letters, 470(3), 239-243 (2000)
Elizabeth S Ingham et al.
The Journal of comparative neurology, 516(2), 125-140 (2009-07-04)
In mammals, non-image-forming visual functions, including circadian photoentrainment and the pupillary light reflex, are thought to be mediated by the combination of rods, cones, and the melanopsin-expressing intrinsically photosensitive retinal ganglion cells (ipRGCs). Although several genetic models have been developed
Fiorenzo Stirpe, Douglas Lappi
Ribosome-inactivating Proteins: Ricin and Related Proteins (2014)
Characterization of the maize b-32 ribosome inactivating protein and its interaction with fungal pathogen development
Chiara Lanzanova
Maydica, 56.1 (2012)
R Iglesias et al.
FEBS letters, 325(3), 291-294 (1993-07-05)
The type 1 ribosome-inactivating protein (RIP) saporin 5 isolated from seeds of Saponaria officinalis L. strongly inhibited translation carried out by Vicia sativa L. purified ribosomes. The toxin multidepurinated V. sativa rRNA, which upon treatment with acid aniline releases several
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