Rabbit Polyclonal RICI antibody. Suitable for EM, ELISA, WB and reacts with Castor bean samples. Cited in 4 publications.
pH: 7.4
Preservative: 0.097% Sodium azide
Constituents: 2.9% Sodium chloride, 0.0268% PBS
| EM | ELISA | WB | |
|---|---|---|---|
| Castor bean | Expected | 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 - |
| 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 EM, ELISA, WB and reacts with Castor bean samples. Cited in 4 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
Ricin toxin A chain also known as RTA or RTA64 works as the enzymatically active part of the ricin toxin. It has a molecular mass of about 32 kilodaltons. RTA is found in Ricinus communis commonly known as the castor bean plant where it binds to ribosomes in eukaryotic cells. RTA inactivates these ribosomes by specifically depurinating the 28S rRNA component stopping protein synthesis and causing cell death. This catalytic activity sets it apart as a highly potent ribosome-inactivating protein.
RTA participates in the toxic action of ricin which is a heterodimeric complex composed of the A chain and the B chain (RTB). RTB assists in binding and entry into host cells while RTA performs the disruptive enzymatic attack on the ribosomes. The severe effects of ricin toxicity depend largely on the function of RTA as it effectively stops cellular machinery leading to cell apoptosis. Understanding these interactions is important for comprehending the biological potential of RTA.
RTA mainly impacts the pathway of protein synthesis in cells. Disruption occurs upon RTA's enzymatic cleavage of the rRNA from the ribosome inhibiting translation initiation and elongation phases in the cellular protein production line. While ricin acts mostly independently some proteins like elongation factors are indirectly affected by this pathway interference. RTA's role in the inhibition of protein synthesis pathways has been a subject of interest especially in studies of eukaryotic cell biology.
RTA's role is mostly associated with its toxic nature rather than regular biological processes. Ricin exposure leads to severe respiratory or gastrointestinal distress depending on the exposure route and contributes to poisoning a public health concern due to potential use in bioterrorism. Protein interactions relevant to such scenarios include connections with additive proteins like other ribosome-inactivating proteins which can amplify the toxic effect. Understanding RTA and its interaction with tissue cells is key to developing countermeasures against its toxic effects.
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