DPP7 assay kit
- Known as:
- DPP7 test reagent
- Catalog number:
- 80207
- Product Quantity:
- 100 reactions
- Category:
- Peptides
- Supplier:
- BPS Bioscience
- Gene target:
- DPP7 assay kit
Related genes to: DPP7 assay kit
- 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: DPP7 assay kit
Human ELC ELISA KIT 96 TEST
OxiSelect Hydroxyl Radical Antioxidant Capacity (HORAC) Activity Assay, Trial Size
OxiSelect In Vitro ROS/RNS Assay Kit (Green Fluorescence), Trial Size
OxiSelect Methylglyoxal (MG) Competitive ELISA Kit
OxiSelect Methylglyoxal (MG) Competitive ELISA Kit
OxiSelect TBARS Assay Kit (MDA Quantitation), Trial Size
OxiSelect Total Antioxidant Capacity (TAC) Assay Kit, Trial Size
OxiSelect™ In Vitro ROS RNS Assay Kit (Green Fluorescence), Trial Size(1-Kit )11,12-EET DHET Immunoassay Kit(1-Kit )11,12-EET_DHET Immunoassay Kit(1-Kit) 11,12-DHET Immunoassay Kit(1-Kit) 14,15-DHET Human Urine ELISA Kit(1-Kit) 14,15-DHET Hypertension ELISA Kit(1-Kit) 14,15-DHET sEH activity ELISA Kit(1-Kit) 14,15-EET DHET Hypertension ELISA Kit Related articles to: DPP7 assay kit
- Disulfidptosis is a recently characterized regulated cell death pathway driven by disulfide stress. However, its immunological consequences in the tumor microenvironment remain poorly defined. In this review, we propose a conceptual framework in which disulfidptosis functions as an immunometabolic rheostat, wherein the net outcome-T cell exhaustion versus immunogenic cell death-is critically dependent on stress intensity, kinetics, and cellular context. We hypothesize that in glucose-deprived gastrointestinal tumors, chronic sub-lethal disulfide stress may erode CD8 T cell effector function through F-actin crosslinking at the immunological synapse, potentially involving STAT3-LDHB-G6PD-driven transcriptional reprogramming toward a TOX-associated exhaustion state. Conversely, acute synchronous tumor lysis releases damage-associated molecular patterns (DAMPs); however, productive dendritic cell (DC) cross-presentation requires that adenosine triphosphate (ATP)/adenosine conversion and high mobility group box 1 (HMGB1) redox state meet quantitative thresholds. The DPP7-GPX4 axis suppresses disulfidptosis to limit DAMP release and facilitate natural killer (NK) cell evasion, positioning it as a candidate innate immune checkpoint. We advance testable predictions for tuning this rheostat via timed nanodelivery, dietary sensitization, and DPP7/GPX4 targeting, while explicitly distinguishing correlative biomarkers from causal mechanisms. Priority experiments to validate-or falsify-the rheostat hypothesis are outlined. - Source: PubMed
Publication date: 2026/08/27
Li YachaoQiu HuaijueLi ZexingGao Xiang - The prognosis for colorectal cancer (CRC) is poor, and the disease is marked by high rates of morbidity and death, highlighting the need for reliable biomarkers. RNA methylation modifications play important roles in cancer biology. However, the integrated role of m6A/m5C/m1A/m7G modifications in CRC has not been fully characterized and requires further investigation. - Source: PubMed
Publication date: 2026/07/08
Chen RuyueYao ZengwuJiang LixinHu Jinchen - To date, the S46 peptidase family is limited to two members, dipeptidyl-peptidase (DPP)7 and DPP11, which are widely distributed among Gram-negative bacteria and present in both oral and intestinal microbiota. Both peptidases are indispensable for the growth of the periodontopathic bacterium Porphyromonas gingivalis. They have a 40.0% amino acid identity, and exhibit specificity for hydrophobic and acidic P1 residues, respectively. This specificity is associated with S1 Gly in DPP7 and the equivalent residue, Arg, in DPP11. Recent studies have revealed a relaxed P1 specificity of DPP7 even for neutral amino acids and hydrophilic Asn. Thus, the broad utility of DPP7 suggests that the ancestral enzyme of the S46 family resembled DPP7. The aim of the present study was to reconstruct the evolutionary divergence of these two DPPs. DPP7 hydrolyzed the tetrapeptidyl substrate LE-|-MP- and LD-|-MP-4-methylcoumaryl-7-amide (MCA) at 4.0% and 7.3%, respectively, of the efficiency of DPP11, whereas DPP11 did not hydrolyze the DPP7 substrate LN-|-MP-MCA, indicating that DPP7 partially complements the role of DPP11. A single amino acid substitution at the S1 site in DPP7 (Gly666Arg) enhanced hydrolysis toward Asp and Glu to a level higher than that of DPP7 wild-type, while a reverse substitution in DPP11 (Arg673Gly) abolished hydrolytic activities toward all substrates examined. Taken together, DPP7 might represent the ancestral form of S46-family peptidases, from which the dpp11 gene arose through gene duplication and subsequent mutations initiated by Gly666Arg substitution. - Source: PubMed
Publication date: 2026/07/15
Sawase MomoShirakura KanaOhara-Nemoto YukoNishimata HarukaFujita YukoIshikawa TaichiNemoto Takayuki K - Triclosan (TCS), a synthetic broad-spectrum antimicrobial and novel persistent organic pollutant, is detected in over 75% of human urine samples, yet its molecular targets in ulcerative colitis (UC) remain unclear. We integrated network toxicology, multi-cohort machine learning, molecular docking, 100-ns all-atom molecular dynamics (MD) simulation, and single-cell transcriptomics to address this gap.Intersecting UC differentially expressed genes with database-derived TCS targets yielded 479 shared candidate targets; because these databases include indirect and probabilistic associations,this set was treated as hypothesis-generating. KEGG enrichment identified the AGE-RAGE signaling pathway, PPAR signaling, and TNF signaling among the top enriched pathways. LASSO regression and random forest algorithms distilled a 10-gene diagnostic signature that achieved cross-cohort AUC of 0.910-1.000 across six independent GEO datasets, consistent with strong discriminative performance.Molecular docking predicted Vina scores of -7.1 kcal/mol (CYP3A4) and -7.0 kcal/mol (DPP7);redocking and decoy analyses supported protocol specificity but not biochemical binding or inhibition. Over 100 ns of MD simulation, the docked poses remained stable for both targets. Single-cell RNA sequencing GSE214695 independently corroborated cell-type-specific CYP3A4 downregulation in epithelial cells and broad DPP7 upregulation across immune subsets in UC.CellOracle-based in silico perturbation predicted that CYP3A4 suppression would impair cytoplasmic translation, while DPP7 suppression would polarize innate inflammation toward an IL-1β-driven phenotype. Together, these analyses computationally prioritize CYP3A4 and DPP7 as candidate TCS-relevant targets in UC and generate testable hypotheses for future experimental validation; they do not by themselves establish direct target engagement, inhibition, or causal contribution to UC. - Source: PubMed
Publication date: 2026/07/16
Wang JiafengJiang SongsongZhang YingyingGao HaoZhao XiaoqiLiu LixiangLi Zijian - This exploratory pilot study, employing a single-center and cross-sectional design, aimed to characterize urinary protein alterations associated with pediatric metabolic-associated fatty liver disease (MAFLD) and to identify preliminary candidate proteins associated with MAFLD status within a cohort of children with obesity. - Source: PubMed
Publication date: 2026/06/23
Zhang XiaohuiZhu ZhongyiZhou ZhaoxinLiu ChangDu LinaGuo ZiyunPu GuoweiHe QiangYang Yan