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AB79621

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

Key facts

Purity

>70% SDS-PAGE

Expression system

Baculovirus infected Sf9 cells

Tags

Tag free

Applications

SDS-PAGE, FuncS

applications

Biologically active

Yes

Biological activity

Specific Activity: 536 U/ug. One U =1 pmol/min.

Accession

Q86TI2

Animal free

No

Carrier free

No

Species

Human

Storage buffer

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

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q86TI2","tags":[]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

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.
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.

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.

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

Product protocols

Target data

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).
See full target information DPP9

Publications (2)

Recent publications for all applications. Explore the full list and refine your search

Frontiers in oncology 11:714527 PubMed34490111

2021

Fluorescence Imaging Using Enzyme-Activatable Probes for Real-Time Identification of Pancreatic Cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Ryugen Takahashi,Takeaki Ishizawa,Masumitsu Sato,Yoshinori Inagaki,Mariko Takanka,Yugo Kuriki,Mako Kamiya,Tetsuo Ushiku,Yasuteru Urano,Kiyoshi Hasegawa

The FEBS journal 282:3737-57 PubMed26175140

2015

Identification of novel dipeptidyl peptidase 9 substrates by two-dimensional differential in-gel electrophoresis.

Applications

Unspecified application

Species

Unspecified reactive species

Hui Zhang,Sadiqa Maqsudi,Adam Rainczuk,Nadine Duffield,Josie Lawrence,Fiona M Keane,Daniela Justa-Schuch,Ruth Geiss-Friedlander,Mark D Gorrell,Andrew N Stephens
View all publications

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