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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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Our Phospho-IGF-I Receptor β (Tyr1135/1136)/Insulin Receptor β (Tyr1150/1151) (19H7) Rabbit mAb #3024 recognizes Tyr1189/1190 in isoform 1 (Long) and Tyr1177/1178 in isoform 2 (Short) of human insulin receptor β (see Uniprot #P06213; https://www.uniprot.org/uniprotkb/P06213/entry#sequences). “Tyr1150/1151” reflects the position of the phosphosites in isoform 2 when the 27 amino acid signal peptide is removed from the N-terminus.