S9896
Saporin Peptide
lyophilized powder, from Saponaria officinalis seeds
Synonym(s):
Saponin Extract
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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 Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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The amino acid sequence of a ribosome-inactivating protein from Saponaria officinalis seeds.
Maras B
Biochemistry International, 21(5), 831-838 (1990)
Analysis of the Sequence Preference of Saporin by Deep Sequencing.
Hauf, et al.
ACS chemical biology, 17, 2619-2630 (2023)
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
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)
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