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The helix-loop-helix transcriptional repressor ID2 is rapidly degraded in mammalian cells. The proteasome is responsible for the bulk of ID2 degradation. It is induced upon IL-4 stimulation of B cells and IL-6 stimulation of fibroblasts. We have used a dominant inhibitor of the 20S proteasome to show that ID2 is not degraded in the proteasome, but that it is degraded in a proteasome-independent manner. We postulate that ID2 is degraded by a kinase-dependent pathway. In the absence of proteasomal activity, ID2 degradation occurs prior to protein turnover and may represent a specific mechanism for establishing and maintaining the repression of factors critical to early B cell differentiation.It is now common practice to package individual packaged products in protective containers which are nested together in a single package. Typically, the manufacturer of these nested packages will seal or wrap the individual packaged products individually with plastic which has an adhesive on its surface. These adhesives generally, but not always, contain an activation step prior to use, and are generally referred to as cold-welding or heat-sealing adhesives. These adhesives generally include two plastic plies which are overlapped and sealed together by the adhesive. This adhesive generally contains a release agent to prevent the adhesive from adhering to the adjacent surfaces of the plastic plies prior to use. These release agents are generally applied to the surface of the plastic plies prior to the initial and subsequent wrapping with the plastic material.
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