Ricin A chain from Ricinus communis (castor bean)

buffered aqueous glycerol solution

Número de CAS:
Número MDL:


buffered aqueous glycerol solution

Nivel de calidad



≥250 μg/mL per mL agglutination activity


Protein, ≥0.3 mg/mL Lowry-TCA

temp. de almacenamiento


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Acciones bioquímicas o fisiológicas

Ricin A chain inactivates the 60 S ribosomal subunit of eukaryotic cells, inhibiting protein synthesis. This toxic activity is independent of the presence of the B chain of ricin.

Otras notas

Ricinus communis toxin (also named RCA60, RCAII, Ricin D, or RCL III) is a highly toxic protein, mol. wt. ~60 kDa, composed of two chains, A and B, connected by a single disulfide bridge.


Electrophoretically pure (SDS-PAGE)

Forma física

Solution in 40% glycerol containing 10 mM phosphate, pH 6.0, 0.15 M NaCl, 10 mM galactose and 0.5 mM dithioerythritol

Nota de preparación

Purified by affinity chromatography.

Nota de análisis

Agglutination activity is expressed in μg/ml and is determined from serial dilutions in phosphate buffered saline, pH 7.2, of a 1 mg/ml solution. This activity is the lowest concentration to agglutinate a 2% suspension of human erythrocytes after 1 hour incubation at 25°C.


Skull and crossbones

Palabra de señalización


Frases de peligro

Equipo de protección personal

Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter


UN 3172 6.1 / PGIII

WGK Alemania


Punto de inflamabilidad F

Not applicable

Punto de inflamabilidad C

Not applicable

Staci Kane et al.
Journal of immunological methods, 451, 54-60 (2017-09-01)
With several ricin contamination incidents reported over the past decade, rapid and accurate methods are needed for environmental sample analysis, especially after decontamination. A sample processing method was developed for common surface sampling devices to improve the limit of detection...
Lisa Fetter et al.
Chemical communications (Cambridge, England), 51(82), 15137-15140 (2015-09-02)
Protein toxins present considerable health risks, but detection often requires laborious analysis. Here, we developed electrochemical aptamer biosensors for ricin and botulinum neurotoxins, which display robust and specific signal at nanomolar concentrations and function in dilute serum. These biosensors may...
Ross Thyer et al.
Nature biotechnology, 36(7), 624-631 (2018-06-05)
Incorporation of the rare amino acid selenocysteine to form diselenide bonds can improve stability and function of synthetic peptide therapeutics. However, application of this approach to recombinant proteins has been hampered by heterogeneous incorporation, low selenoprotein yields, and poor fitness...
Natália L Sousa et al.
Scientific reports, 7(1), 15385-15385 (2017-11-15)
Ricin is a highly toxic ribosome-inactivating lectin occurring in the seeds of castor bean (Ricinus communis L.). Castor bean grows throughout tropical and sub-tropical regions and is a very important crop due to its high seed content of ricinoleic acid...

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