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It is possible to see three bands for the large subunit of cleaved caspase-3. The bands all represent cleavage at Asp175. However, the distinction between the three is the extent of processing at the amino termini of the proteins [see Fernandes-Alnemri, T. et al. (1996) Proc Natl Acad Sci U S A. 93(15), 7464-9 (PMID: 8755496; http://www.ncbi.nlm.nih.gov/pubmed/8755496)]. Processing of caspase-3 into its fully active form is a two-step process. Step 1 involves cleavage at Asp175, which generates the 20 kDa large subunit and the 12 kDa small subunit. In step 2, the 20 kDa large subunit is further cleaved at Asp9, probably through auto-catalytic activity. The removal of the first nine amino acids of the pro-domain results in the 19 kDa subunit. Further cleavage can also occur more slowly at Asp28 to generate the fully mature 17 kDa subunit. Therefore, any accumulation of the 20 and 19 kDa subunits is presumabl…
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While we do not specifically test our antibodies using co-IP, we expect IP-approved antibodies to work well for co-IP experiments. As each protein-protein interaction is unique, optimization of lysis conditions and the inclusion of proper controls are necessary for a successful experiment. More information on experimental design for IP and co-IP experiments can be found here.
For co-IPs, we suggest blotting for the target protein first to confirm pull-down. Once confirmed, blotting for additional proteins in the complex can be performed. If your protein of interest runs at a size similar to the heavy or light chain of IgG, we recommend the use of a conformation-specific or