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Key Documents

S9896

Sigma-Aldrich

Saporin Peptide

lyophilized powder, from Saponaria officinalis seeds

Sinônimo(s):

Saponin Extract

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About This Item

Número MDL:
Código UNSPSC:
12352202
NACRES:
NA.32

product name

Saporin from Saponaria officinalis seeds, lyophilized powder

fonte biológica

plant seeds (Saponaria officinalis)

Nível de qualidade

Ensaio

10.00-30.00%

forma

lyophilized powder

composição

Protein, ~20% Lowry

técnica(s)

activity assay: suitable

temperatura de armazenamento

2-8°C

Descrição geral

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.

Aplicação

Saporin from Saponaria officinalis seeds has been used to study its antifungal activity against Fusarium verticillioides.

Ações bioquímicas/fisiológicas

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.

Embalagem

Package size based on protein content.

forma física

Lyophilized powder containing glucose and sodium phosphate buffer salts

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)


Certificados de análise (COA)

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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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