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RTA | Ricin toxic A chain

AS17 4143   | Clonality: Polyclonal  |  Host: Rabbit | Reactivity: Ricinus communis

RTA | Ricin toxic A chain  in the group Antibodies for Plant/Algal / Toxins / Plant toxins at Agrisera AB (Antibodies for research) (AS17 4143)

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product information
Background Ricin is a naturally occuring protein found in castor bean (Ricinus communis) acting as protein synthesis inhibitor. It is a toxin involved in plant defence. A chain of ricin can inactivate few thousands of ribosomes per minute. B chain facilitates the entry of A chain into the cell. Both protein chains, A and B must be present in order to produce an active toxin.

Ricin toxic A chain is an N-glycosylated heterodimer of approximately 60 to 65 kDa.
Immunogen Ricin A chain isolated from Ricinus communis var. Impala
Host Rabbit
Clonality Polyclonal
Clone
Purity Serum
Format Lyophilized
Quantity 50 µl
Reconstitution For reconstitution add 50 µl of sterile water.
Storage

Lyophilized antibody can be stored at -20°C for up to 3 years. Re-constituted antibody can be stored at 4°C for several days to weeks.
Once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please, remember to spin tubes briefly prior to opening them to avoid any losses that might occur from lyophilized material adhering to the cap or sides of the tubes.

Tested applications ELISA (ELISA)
Related products AS17 4144 | Anti-RTB | Ricin toxic B chain rabbit antibodies
AS09 648
| Anti-Ricin (RTA subunit), clone MMA, mouse monoclonal antibody
AS09 649 | Anti-Ricin (whole molecule), clone MMH, mouse monoclonal antibody
Additional information
application information
Recommended dilution

1: 10 000 (ELISA)

Expected | apparent MW
Confirmed reactivity Ricinus communis
Predicted reactivity
Not reactive in

No confirmed exceptions from predicted reactivity are currently known

Additional information Antibody is recognizing active toxin complex containing both, ricin A and B subunits.
Selected references

To be added when available, antibody available in December 2017.



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