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S9896

Sigma-Aldrich

Saporin from Saponaria officinalis seeds

lyophilized powder

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MDL number:
NACRES:
NA.32

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

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Saponin from quillaja bark Sapogenin content ≥10 %

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assay

10.00-30.00%

assay

≥98% (PAGE)

assay

≥95% (HPLC)

assay

-

technique(s)

activity assay: suitable

technique(s)

activity assay: suitable

technique(s)

-

technique(s)

HPLC: suitable, protein quantification: suitable

Quality Level

200

Quality Level

300

Quality Level

200

Quality Level

-

form

lyophilized powder

form

essentially salt-free, lyophilized powder

form

-

form

-

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

-

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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Analysis of the Sequence Preference of Saporin by Deep Sequencing.
Hauf, et al.
ACS chemical biology, 17, 2619-2630 (2023)
A P Fordham-Skelton et al.
Molecular & general genetics : MGG, 229(3), 460-466 (1991-10-01)
A. Saponaria (soapwort) genomic library was screened with a PCR-derived saporin-specific gene probe. The nucleotide sequences of three saporin genomic clones were determined. One of the clones contained a full-length saporin coding sequence whilst the other two were truncated. A
Characterization of the maize b-32 ribosome inactivating protein and its interaction with fungal pathogen development
Chiara Lanzanova
Maydica, 56.1 (2012)
Fiorenzo Stirpe, Douglas Lappi
Ribosome-inactivating Proteins: Ricin and Related Proteins (2014)
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

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