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Merck

Antibody proteolysis: a common picture emerging from plants.

Bioengineered (2015-07-18)
Marcello Donini, Raffaele Lombardi, Chiara Lonoce, Mariasole Di Carli, Carla Marusic, Veronica Morea, Patrizio Di Micco
ABSTRACT

We have recently characterized the degradation profiles of 2 human IgG1 monoclonal antibodies, the tumor-targeting mAb H10 and the anti-HIV mAb 2G12. Both mAbs were produced in plants either as stable transgenics or using a transient expression system based on leaf agroinfiltration. The purified antibodies were separated by 1DE and protein bands were characterized by N-terminal sequencing. The proteolytic cleavage sites identified in the heavy chain (HC) of both antibodies were localized in 3 inter-domain regions, suggesting that the number of proteolytic cleavage events taking place in plants is limited. One of the cleavage sites, close to the hinge region, was common to both antibodies.

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Sigma-Aldrich
Anti-Human Lambda Light Chains (Bound and Free)−Peroxidase antibody produced in goat, affinity isolated antibody, buffered aqueous solution