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Merck

S9896

Sigma-Aldrich

Saporin Peptide

lyophilized powder, from Saponaria officinalis seeds

Sinónimos:

Saponin Extract

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About This Item

MDL number:
UNSPSC Code:
12352202
NACRES:
NA.32

product name

Saporin from Saponaria officinalis seeds, lyophilized powder

biological source

plant seeds (Saponaria officinalis)

Quality Level

assay

10.00-30.00%

form

lyophilized powder

composition

Protein, ~20% Lowry

technique(s)

activity assay: suitable

storage temp.

2-8°C

General description

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.

Biochem/physiol Actions

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.

Packaging

Package size based on protein content.

Physical form

Lyophilized powder containing glucose and sodium phosphate buffer salts

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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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