DPP2 antibody Polyclonal Antibodies Primary antibodies
- Known as:
- DPP2 (anti-) Polyclonal Antibodies Primary antibodies
- Catalog number:
- orb101086
- Product Quantity:
- 100
- Category:
- -
- Supplier:
- Biorb
- Gene target:
- DPP2 antibody Polyclonal Antibodies Primary antibodies
Related genes to: DPP2 antibody Polyclonal Antibodies Primary antibodies
- Gene:
- DPP7 NIH gene
- Name:
- dipeptidyl peptidase 7
- Previous symbol:
- -
- Synonyms:
- DPPII, DPP2
- Chromosome:
- 9q34.3
- Locus Type:
- gene with protein product
- Date approved:
- 2001-04-20
- Date modifiied:
- 2016-02-08
Related products to: DPP2 antibody Polyclonal Antibodies Primary antibodies
Related articles to: DPP2 antibody Polyclonal Antibodies Primary antibodies
- Metabolic dysfunction-associated fatty liver disease (MASLD) is a highly prevalent liver condition with a complex etiology increasingly linked to air pollution. However, the molecular mechanisms through which air pollutants exacerbate MASLD remain poorly understood. In this study, we integrated computational toxicology, multi-omics analyses, and machine learning to identify critical molecular targets of hepatotoxicity-related air pollutants (HTRAPs). This integrated approach identified ozone (O) and carbon monoxide (CO) as HTRAPs based on their hepatotoxic potential. Using integrative machine learning, we pinpointed Cathepsin G (CTSG), Dipeptidyl Peptidase 7 (DPP7), and Apolipoprotein B MRNA Editing Enzyme Catalytic Subunit 3G (APOBEC3G) as key MASLD-related targets. To validate these findings, we measured the dysregulated expression of critical genes in MASLD-simulating cells treated with O using quantitative real-time PCR (qRT-PCR). Molecular docking and dynamics simulations indicated a high-affinity, potential binding mode between O and the CTSG protein. High CTSG expression correlated with neutrophil infiltration and neutrophil extracellular traps (NETs) formation. Interestingly, a significant positive correlation was observed between NETs formation and the enrichment of regulatory B cells. This study proposes a novel hypothesis that O may facilitate NETs formation by interacting with CTSG. These findings highlight CTSG as a potential therapeutic target and underscore the role of air pollution in MASLD progression. - Source: PubMed
Publication date: 2026/05/11
Hou YingdongWang ZhijieZhang Xiaofeng - Dipeptidyl-peptidases (DPPs), including the S9-family DPP4 and DPP5 and the S46-family DPP7 and DPP11, are essential for growth of Porphyromonas gingivalis, a periodontopathic bacterium associated with systemic diseases. DPPs release dipeptides in diverse combinations from peptidyl N-termini, thus enabling utilization of amino acids as carbon and energy sources. This study examined how DPP5 and DPP7 achieve division of labor despite both possessing preference for hydrophobic residues at the P1 and P2 substrate positions. To identify important positions of substrates that define the specificity of DPPs, the terms coefficient of variation in amino acid frequency and coefficient of variation in protease activity (CVA) are introduced, as the values increase when a substrate position more strongly affects enzyme activity. In particular, CVA was found useful for peptidases, such as DPPs, for which a limited number of substrates are available. Using HX-|-LD-4-methylcoumaryl-7-amide (MCA), XN-|-LD-MCA, and XN-|-SD-MCA (X = nine amino acids) as substrates, DPP5 and DPP7 exhibited higher CVA values at the P1 and P2 positions, respectively, than at their counter positions. Furthermore, least-squares method applied on the relationship between peptidase activity and hydrophobicity for 27 dipeptidyl-MCA substrates independently indicated the best fit for DPP5 at 100% P1 and 0% P2, and for DPP7 at 53% P1 and 47% P2. Both approaches showed that functional division of labor is achieved through the exclusive P1 preference of DPP5 and the unusual P2 significance for DPP7. These results also demonstrate the usefulness of CVA for evaluating positional effects of substrates in peptidase reactions. - Source: PubMed
Publication date: 2026/05/12
Sawase MomoShirakura KanaOhara-Nemoto YukoNishimata HarukaKondo HisayoshiIshikawa TaichiFujita YukoNemoto Takayuki K - Colorectal cancer (CRC) is a leading cause of cancer mortality. The Golgi apparatus (GA) mediates protein glycosylation and secretion, and its dysfunction is implicated in cancer invasion and immune evasion [1]. The prognostic relevance of GA-related genes in CRC remains unclear. - Source: PubMed
Publication date: 2026/05/09
Wu Shuaiyi - Porphyromonas gingivalis is the most common periodontal pathogen. P. gingivalis dipeptidyl peptidase 7 (PgDPP7) belongs to a new class of serine peptidases, family S46. S46 peptidases are absent in mammals. Therefore, these enzymes are promising targets for novel antibacterial agents. In this study, inhibitors were designed based on the cocrystal structures of valyl-tyrosine and phenylalanyl-tyrosine, which bind to the active centers of DPP7 derived from bacteria, and dipeptide derivatives that inhibit PgDPP7 were obtained. The active compound KGDI-109, the first peptidyl inhibitor of S46 peptidases, exerted an inhibitory effect against P. gingivalis growth at a minimum inhibitory concentration of 1.56 µM. In C57BL/6 N male mice with induced periodontitis, the oral administration of KGDI-109 significantly suppressed alveolar bone resorption and reduced the amount of P. gingivalis in the oral cavity, indicating that the DPP inhibitor suppresses periodontal disease by its antibacterial activity. This dipeptide derivative did not inhibit the growth of other oral bacteria, and its antibacterial action was presumed to target bacteria possessing DPP, particularly P. gingivalis. Furthermore, KGDI-109 may be more effective than azithromycin in maintaining the gut microbial diversity and reducing adverse health effects. KGDI-109 can be a novel treatment for periodontal diseases targeting P. gingivalis. - Source: PubMed
Publication date: 2026/05/08
Aoki-Nonaka YukariMinato YukakoHidaka KoushiWarita YukoAndo DaikiLwin Hnin YuMatsugishi-Nasu AoiTakahashi NaokiNakamura AkihiroOgasawara WataruSekiya MizukiSakamoto YasumitsuTabeta Koichi - Benzo(a)pyrene (BaP), an environmental carcinogen, contributes to colon cancer pathogenesis through incompletely elucidated mechanisms. This study integrated network toxicology and multi-omics analyses to decipher BaP-associated molecular signatures and clinical relevance in colon cancer. Using TCGA-COAD data, 113 differentially expressed BaP-related targets were identified via CTD and Super-PRED databases. PPI networks, functional enrichment, and Cox/Lasso regression revealed key pathways (xenobiotic metabolism, p53 signaling, cell cycle) and six prognostic genes (CLK2, CRYAB, RPS6KA1, DPP7, CDC25C, GAST). A BaP-related risk model stratified patients into distinct survival groups. A nomogram accurately predicted 1-, 3-, and 5-year overall survival. High-risk scores correlated with advanced tumor stage, metastasis, and immunosuppressive microenvironments. Molecular docking demonstrated strong BaP binding to CLK2 and CRYAB. External validation (GSE39582, TNMplot) confirmed tumor-specific gene expression patterns. These findings delineate BaP-driven networks connecting xenobiotic stress, immune dysregulation, and tumor progression. The risk model provides a prognostic biomarker for personalized management and therapeutic targeting in colon cancer. - Source: PubMed
Publication date: 2026/04/22
Yang XueyingYang ZhendongSui Bowen