Tissue Specificity | Ubiquitously expressed, with highest levels in liver, heart and muscle, and lowest levels in brain. |
Function | Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. Acts as a key inhibitor of caspase-1-dependent monocyte and macrophage pyroptosis in resting cells by preventing activation of NLRP1 and CARD8. Sequesters the cleaved C-terminal part of NLRP1 and CARD8, which respectively constitute the active part of the NLRP1 and CARD8 inflammasomes, in a ternary complex, thereby preventing their oligomerization and activation. The dipeptidyl peptidase activity is required to suppress NLRP1 and CARD8.however, neither NLRP1 nor CARD8 are bona fide substrates of DPP9, suggesting the existence of substrate(s) required for NLRP1 and CARD8 inhibition. |
Protein Name | Dipeptidyl Peptidase 9Dp9Dipeptidyl Peptidase Iv-Related Protein 2Dprp-2Dipeptidyl Peptidase IxDpp IxDipeptidyl Peptidase-Like Protein 9Dplp9 |
Cellular Localisation | Isoform 1: CytoplasmCytosolIsoform 2: Nucleus |
Alternative Antibody Names | Anti-Dipeptidyl Peptidase 9 antibodyAnti-Dp9 antibodyAnti-Dipeptidyl Peptidase Iv-Related Protein 2 antibodyAnti-Dprp-2 antibodyAnti-Dipeptidyl Peptidase Ix antibodyAnti-Dpp Ix antibodyAnti-Dipeptidyl Peptidase-Like Protein 9 antibodyAnti-Dplp9 antibodyAnti-DPP9 antibodyAnti-DPRP2 antibody |
Information sourced from Uniprot.org