Rabbit Polyclonal RICI antibody. Suitable for ELISA, WB and reacts with Castor bean samples. Cited in 2 publications.
pH: 7.4
Preservative: 0.097% Sodium azide
Constituents: 2.9% Sodium chloride, 0.0268% PBS
ELISA | WB | |
---|---|---|
Castor bean | Expected | Expected |
Species | Dilution info | Notes |
---|---|---|
Species Castor bean | Dilution info Use at an assay dependent concentration. | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Castor bean | Dilution info Use at an assay dependent concentration. | Notes - |
Ricin is highly toxic to animal cells, and to a lesser extent to plant cells. Ricin A chain. Acts as a glycosidase that removes a specific adenine residue from an exposed loop of the 28S rRNA (A4324 in mammals), leading to rRNA breakage. As this loop is involved in elongation factor binding, modified ribosomes are catalytically inactive and unable to support protein synthesis. Can inactivate a few thousand ribosomes per minute, faster than the cell can make new ones. Therefore a single molecule can kill an animal cell. Ricin B chain. Binds to beta-D-galactopyranoside moieties on cell surface glycoproteins and glycolipids and facilitates the entry into the cell of the A chain. Also responsible for cell agglutination (Lectin activity).
Ricin
Rabbit Polyclonal RICI antibody. Suitable for ELISA, WB and reacts with Castor bean samples. Cited in 2 publications.
pH: 7.4
Preservative: 0.097% Sodium azide
Constituents: 2.9% Sodium chloride, 0.0268% PBS
sterile-filtered (0.22 mm pore size) serum with the addition of 15 mM NaN3.
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Ricin toxin B chain also known as R. communis agglutinin B-chain plays an important mechanical role in the facilitation of toxin entry into cells. This B chain is part of the ricin toxin dimer a toxic protein originating from the seeds of the castor oil plant. It possesses a mass of approximately 34 kDa. The B chain specifically binds to galactose residues on cell surface glycoproteins and glycolipids enabling the internalization of the toxin into the cells. Expression is found in the seed endosperm of Ricinus communis where the protein functions as part of the natural defense mechanism of the plant.
The Ricin toxin B chain participates in the entry phase of the ricin toxin's mechanism. As a component of the ricin toxin dimer complex it works alongside the A chain which exerts catalytic activity leading to cellular damage. The B chain’s function is largely supportive providing the binding feature to target and deliver the A chain into the cell. This process involves endocytosis where the toxin exploits cellular mechanisms using a vesicular transport system to reach the endoplasmic reticulum before the A chain disengages to disrupt protein synthesis.
Scientists observe that the Ricin toxin B chain uniquely operates within cellular uptake and trafficking systems. It manipulates the endocytic pathway to achieve cellular penetration and transport to its functional site. The B chain's engagement with the retrograde transport pathway highlights its interaction with proteins like clathrin and components of the trans-Golgi network. This pathway not only facilitates the transport of ricin toxin but also shares similarities with pathways used by cholera toxin for host cell entry.
Researchers have discovered the toxic properties of the Ricin toxin B chain contribute to its potential use in developing cancer therapies. The chain’s precise binding to cell surface carbohydrates could be harnessed for targeted therapy delivery systems. Additionally concerns over ricin toxin's use as a bioterrorism agent have highlighted its relation to hazardous exposure cases. The chain's action associates with proteins involved in protein synthesis inhibition increasing understanding of how cell sharpshooter approaches could target proliferative diseases like cancer using the B chain for specific and effective therapeutic applications.
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