Canp enzyme was isolated from Drosophila adults. The enzyme is absolutely Ca2+-dependent and shows the inhibitor pattern of thiol proteases. Several of its properties resemble those of vertebrate calpain II, however no analog of the vertebrate calpain II small subunit was found.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Canp using the Feature Mapper tool.
GBrowse - Visual display of RNA-Seq signalsView Dmel\Canp in GBrowse 2
Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.
For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.
"Canp" (purified and studied in FBrf0055463) is not the same as "CalpI" (partially purified and studied in FBrf0047562). The relationship between "Canp" and "CalpII" (partially purified and studied in FBrf0047562) is unknown. "Canp" is unlikely to be the same as "CalpA", since "Canp" protein is purified from the cytosol and "CalpA" is not detected in the cytosol with an anti-"CalpA" antibody.