Caspase Fluorometric Substrate Set7 x 25 assays
- Known as:
- Caspase Fluorometric Substrate Set7 x 25 tests
- Catalog number:
- K131-7-25
- Product Quantity:
- 7 x 25 assays
- Category:
- Peptides
- Supplier:
- Biovis
- Gene target:
- Caspase Fluorometric Substrate Set7 25 assays
Related genes to: Caspase Fluorometric Substrate Set7 x 25 assays
- Gene:
- KMT5A NIH gene
- Name:
- lysine methyltransferase 5A
- Previous symbol:
- SETD8
- Synonyms:
- SET8, SET07, PR-Set7
- Chromosome:
- 12q24.31
- Locus Type:
- gene with protein product
- Date approved:
- 2006-02-15
- Date modifiied:
- 2016-02-12
Related products to: Caspase Fluorometric Substrate Set7 x 25 assays
*Lactobacilli Broth,AOAC USE For preparation of inocula of test bacteria used in microbiological assays of B vitamins.1,2-Dioleoyl-3-(pyren-1-yl) decanoyl-rac-glycerol, Fluorescent Lipase Substrate, 1mg Ampule1,2-Dioleoyl-3-(pyren-1-yl) decanoyl-rac-glycerol, Fluorescent Lipase Substrate, 1mg Ampule1,2_Dioleoyl_3_(pyren_1_yl) decanoyl_rac_glycerol, Fluorescent Lipase Substrate, 1mg Ampule10C6 Caspase 211B4 Caspase 215-PGDH Inhibitor Screening Kit (Fluorometric)1G12 Caspase-81H11 Caspase-11X TMB ELISA Substrate Solution 100 mL2 CDC25C, CHK1 and CHK2 Substrate, phosphorylated2', 7'-Dichlorofluorescin diacetate, Enzyme Substrate, 25mg2', 7'-Dichlorofluorescin diacetate, Enzyme Substrate, 25mg2', 7'_Dichlorofluorescein diacetate, Enzyme Substrate, 25mg2, 7-Dichlorofluorescein di-galactoside, Fluorescent substrate for measuring galactosidase and galactocerebrosidase activity, 25mg Related articles to: Caspase Fluorometric Substrate Set7 x 25 assays
- Hepatocellular carcinoma has poor prognosis due to its high recurrence rate, even after curative surgery. Epigenetic regulators are known to play a critical role in cancer progression, and the histone methyltransferase SETD8/KMT5A has been reported to be overexpressed in various malignancies. In this study, we aimed to elucidate the role of SETD8/KMT5A in hepatocellular carcinoma. - Source: PubMed
Publication date: 2026/04/13
Suzaki NorihikoHayami ShinyaMiyamoto AtsushiNakamura MasashiYoshimura TomohiroNakamura KensukeShigekawa YoshinobuShimizu AtsushiKitahata YujiTakeuchi AkihiroMotobayashi HidekiOsada ShigehiroEhata ShogoHamamoto RyujiKawai Manabu - KMT5a, a histone lysine methyltransferase responsible for histone H4 lysine 20 monomethylation (H4K20me1), plays a critical role in the pathogenesis of various human diseases, including cancer. In glioblastoma, KMT5a is frequently overexpressed, with elevated expression levels correlating with poor clinical outcomes, and its inhibition restrains cell growth. The KMT5a-induced H4K20 methylation regulates the expression of several oncogenes and tumor suppressor genes, but its transcriptional targets in glioblastoma remain poorly understood. Through RNA-sequencing, we found that the expression of the key autophagy adaptor was strongly repressed by KMT5a. - Source: PubMed
Publication date: 2026/03/13
Della Monica RosaBuonaiuto MichelaCuomo MariellaDrongitis DeniseMiano Maria GiuseppinaCostabile Davidede Riso GiuliaTrio FedericaSabbarese MartaFerraro SaraOliva LorenzaPiacentino NivesCappiello RosariaScotti GianlucaLasorsa Vito AlessandroCapasso MarioDe Bellis AlbertoDel Basso De Caro MarialauraChiariotti LorenzoVisconti Roberta - Depending upon the type of pathological stress, the heart undergoes concentric or eccentric remodeling. This structural change is associated with diastolic and/or systolic ventricular dysfunction reflecting differentially altered cardiomyocyte morphology, ultrastructure, metabolism, contractility, and survival, as well as interstitial myocardial fibrosis. Despite an association of both concentric and eccentric remodeling with heart failure and sudden death, the molecular mechanisms resulting in abnormal cardiac geometry remain poorly understood. A better understanding of the basic mechanisms conferring these contrasting forms of remodeling should inform novel approaches to preserve normal cardiac structure and function in cardiovascular disease. The protein phosphatase Cell Division Cycle 14A (CDC14A) and its substrate the lysine methyltransferase KMT5A are identified herein as key regulators of the balance between concentric and eccentric pathological cardiac remodeling. - Source: PubMed
Publication date: 2026/02/17
Li XueyiLi JinliangTan YuliangSamuelsson Anne-MajNguyen Vi BNair Ramesh VColombe Anne-SophieGrimm DirkRosenfeld Michael GKapiloff Michael S - SET domain containing 5 (SETD5), a chromatin regulator involved in adipocytic differentiation, has been identified in various cancers, but its immunohistochemical expression and prognostic significance in liposarcoma remain unclear. This study examined the immunohistochemical expression and prognostic significance of SETD5 in liposarcomas. SETD5 expression was analyzed in 100 adipocytic tumors using immunohistochemistry; these 100 tumors consisted of 24 dedifferentiated liposarcomas (DDLPS), 24 atypical lipomatous tumors/well differentiated liposarcomas (WDLPS), 12 myxoid liposarcomas, 5 pleomorphic liposarcomas, and 35 benign adipocytic tumors. SETD5 expression was assessed using the immunoreactivity score and its prognostic significance was investigated. SETD5 expression was absent in normal adipose tissue and minimal in lipomas. SETD5 expression was significantly higher in WDLPS than in lipomas (p = 0.01). Moreover, SETD5 expression was markedly elevated in the dedifferentiated component of DDLPS compared to the well-differentiated component (p < 0.001). Pleomorphic liposarcoma showed the highest SETD5 expression levels. In DDLPS, high SETD5 expression in the dedifferentiated component correlated with worse overall survival (p < 0.001) but was not correlated with disease-free survival (p = 0.086). Immunohistochemical expression of SETD5 significantly correlates with prognosis in DDLPS and may serve as a candidate pathological factor for dedifferentiation and prognosis. - Source: PubMed
Publication date: 2025/12/30
Abe MakotoKubota NaotoYamazaki KenMiura EisukeHirabayashi KaoruIshii MasatsuguShirakawa HirofumiKikuta KazutakaMurayama YudaiNakagawa RumiOjima Hidenori - Hypoxia is a hallmark of the tumor microenvironment that profoundly alters the cellular metabolism and epigenetic regulation. In this study, we investigated how oxygen limitation reprograms histone methylation in glioblastoma cells by integrating stable isotope tracing with high-resolution proteomics and epigenomics. Using deuterium-labeled serine and the RQMID-MS platform, we demonstrated that hypoxia impairs methyl group transfer from serine to histones due to the downregulation of the vitamin B transporter TCN2, which is critical for homocysteine remethylation and SAM synthesis. Despite this blockade in one-carbon metabolism, global histone methylation patterns were not uniformly suppressed. Instead, we observed site-specific changes driven by altered expression of methyltransferases and demethylases, particularly decreased KMT1F (H3K9 methylation) and KMT2B (H3K4 methylation) and increased KDM2A (H3K36 demethylation), KDM3A (H3K9 demethylation), and KMT5A/SETD8 (H4K20 monomethylation). These findings reveal that the histone methylation landscape under hypoxia is governed by a compensatory interplay between one-carbon metabolism and chromatin-modifying enzyme regulation. - Source: PubMed
Publication date: 2025/11/26
Tang HuiXu PeiHerring JasonZhang Kangling