S9896
Saporin from Saponaria officinalis seeds
lyophilized powder
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About This Item
origen biológico
plant seeds (Saponaria officinalis)
Nivel de calidad
Análisis
10.00-30.00%
formulario
lyophilized powder
composición
Protein, ~20% Lowry
técnicas
activity assay: suitable
temp. de almacenamiento
2-8°C
Descripción general
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.
Aplicación
Saporin from Saponaria officinalis seeds has been used to study its antifungal activity against Fusarium verticillioides.
Acciones bioquímicas o 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.
Envase
Package size based on protein content.
Forma física
Lyophilized powder containing glucose and sodium phosphate buffer salts
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
Eyeshields, Gloves, type N95 (US)
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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The crystal structure of saporin SO6 from Saponaria officinalis and its interaction with the ribosome.
Febs Letters, 470(3), 239-243 (2000)
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
Ribosome-inactivating Proteins: Ricin and Related Proteins (2014)
Characterization of the maize b-32 ribosome inactivating protein and its interaction with fungal pathogen development
Maydica, 56.1 (2012)
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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