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Key Documents

S9896

Sigma-Aldrich

Saporin Peptide

lyophilized powder, from Saponaria officinalis seeds

Synonyme(s) :

Saponin Extract

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About This Item

Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32

product name

Saporin from Saponaria officinalis seeds, lyophilized powder

Source biologique

plant seeds (Saponaria officinalis)

Niveau de qualité

Pureté

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)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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
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
The crystal structure of saporin SO6 from Saponaria officinalis and its interaction with the ribosome.
Savino C
Febs Letters, 470(3), 239-243 (2000)
Fiorenzo Stirpe, Douglas Lappi
Ribosome-inactivating Proteins: Ricin and Related Proteins (2014)

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