Recombinant human DPP9 protein
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(2 Publications)
Recombinant human DPP9 protein is a Human Full Length protein, expressed in Baculovirus infected Sf9 cells, with >70%, suitable for SDS-PAGE, FuncS.
View Alternative Names
DPRP2, DPP9, Dipeptidyl peptidase 9, DP9, Dipeptidyl peptidase IV-related protein 2, Dipeptidyl peptidase IX, Dipeptidyl peptidase-like protein 9, DPRP-2, DPP IX, DPLP9
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
DPP9 acts in several processes beyond simple protease activity. It modulates antigen presentation and immune responses. It functions mainly intracellularly and is not typically secreted. While DPP9 does not form stable complexes with other proteins it does interact dynamically with several cellular proteins to perform its roles. Its enzyme activity can regulate peptide hormones and chemokines implicating it in immune modulation.
Pathways
DPP9 plays roles in the regulation of insulin signaling and immune system pathways. It modulates the activity of proteins like fibroblast growth factor (FGF) and is directly involved in the processing of bioactive peptides related to the immune response. DPP9 shares functional traits with DPP8 another member of the dipeptidyl peptidase family which also cleaves similar substrates and participates in overlapping pathways.
Specifications
Form
Liquid
Additional notes
Affinity purified.
General info
Function
Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2 (PubMed : 12662155, PubMed : 16475979, PubMed : 19667070, PubMed : 29382749, PubMed : 30291141, PubMed : 33731929, PubMed : 36112693). Acts as a key inhibitor of caspase-1-dependent monocyte and macrophage pyroptosis in resting cells by preventing activation of NLRP1 and CARD8 (PubMed : 27820798, PubMed : 29967349, PubMed : 30291141, PubMed : 31525884, PubMed : 32796818, PubMed : 36112693, PubMed : 36357533). 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 (PubMed : 33731929, PubMed : 33731932, PubMed : 34019797). 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 (PubMed : 33731929).
Sequence similarities
Belongs to the peptidase S9B family. DPPIV subfamily.
Subcellular localisation
Nucleus
Target data
Publications (2)
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Frontiers in oncology 11:714527 PubMed34490111
2021
Applications
Unspecified application
Species
Unspecified reactive species
The FEBS journal 282:3737-57 PubMed26175140
2015
Applications
Unspecified application
Species
Unspecified reactive species
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