Resources results for "K19"
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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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MAFA is a phosphoprotein. The multiple phosphorylation sites on this protein cause a mobility shift, resulting in the protein migrating slower by gel electrophoresis. This has been confirmed by treatment with CIAP, which has been shown to result in a shift in MAFA’s mobility from approximately 48 kDa to a more rapidly migrating form of approximately 40 kDa (see PMID: 17682063 Figure 1A; https://pubmed.ncbi.nlm.nih.gov/17682063/).
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SRPK2 generally never migrates at its predicted molecular weight (MW) due to post-translational modifications including, but not limited to, phosphorylation. The ~70 kDa band observed by the total antibodies is likely the C-terminal cleavage product. The SRPK2 protein is cleaved at D139 and D403, allowing the N-terminal fragments to travel to the nucleus. Please refer to Figure 3 in this article for more information. Notably, C-terminal phosphorylation of SRPK2 at T492 by Akt seems to prevent this cleavage, so it is uncommon to observe any of the lower MW fragments using a C-terminal phospho-specific SRPK2 antibody.
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The Bcl-xL (54H6) Rabbit mAb #2764 recognizes a portion of the human Bcl-xL sequence which is retained in all three isoforms of Bcl-xL. Please see UniProt for the precise isoform sequences:
https://www.uniprot.org/uniprot/Q07817#sequences
The doublet is most likely Bcl-xL and Bcl-xB, as Bcl-xS has a lower predicted molecular weight (19 kDa versus 25-26 kDa).