Recombinant human DPP9 protein is a Human Full Length protein, expressed in Baculovirus infected Sf9, with >70% purity and suitable for SDS-PAGE, FuncS.
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
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).
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
Recombinant human DPP9 protein is a Human Full Length protein, expressed in Baculovirus infected Sf9, with >70% purity and suitable for SDS-PAGE, FuncS.
pH: 8
Constituents: 50% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.395% Tris HCl, 0.05% Sorbitan monolaurate, ethoxylated, 0.0462% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
Affinity purified.
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).
Belongs to the peptidase S9B family. DPPIV subfamily.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Dipeptidyl peptidase 9 (DPP9) is an intracellular serine protease belonging to the S9B family primarily recognized for its enzymatic function of cleaving dipeptides from polypeptides. It is known alternatively as DPPIV-like protease with a molecular weight of approximately 92 kDa. DPP9 is expressed in multiple tissues with higher levels seen in the liver kidney and lung. Its role is critical for processing proteins influencing their maturation and function.
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.
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.
DPP9 is implicated in certain cancers and inflammatory diseases. For instance its dysregulation correlates with hepatocellular carcinoma. High DPP9 expression is also linked to inflammatory diseases where immune system alterations are pronounced. DPP4 a related enzyme also participates in these conditions highlighting potential therapeutic intervention points targeting both DPP9 and DPP4.
We are dedicated to supporting your work with high quality reagents and we are here for you every step of the way should you need us.
In the unlikely event of one of our products not working as expected, you are covered by our product promise.
Full details and terms and conditions can be found here:
Terms & Conditions.
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com