recombinant human hdac5  (BPS Bioscience)

Journal: Scientific Reports

Article Title: Epigenetic, neuroplasticity, and adrenergic targets associated with major depression in immune cells

doi: 10.1038/s41598-026-36954-9

Figure Lengend Snippet: Cellular distribution of HDAC5 immunofluorescence in the three subsets of monocytes and T-cells. ( A ) Representative field of monocytes and T-cells in 2D, (magnification 40x, scale bar 20 μm). ( B ) Representative photomicrographs in 3D of a classic monocyte for HDAC5+ (green) DAPI+ (blue) and double (HDAC5+/DAPI+) immunofluorescence in classic, intermediate and non-classic monocytes and T-cells. ( C ) HDAC5 immunofluorescence intensity in the nucleus and in the cytoplasm of the three subsets of monocytes and T-cells of HC ( n = 50) and MD patients ( n = 54 MD). For analysis of monocyte subsets two-way ANOVA was used; *** p < 0.001 as indicated; *** in blue, p < 0.001 versus corresponding nuclear compartment (Sidak´s test). For T-cells, *** p < 0.001 versus corresponding nuclear compartment (Student´s t-test). HC: healthy control; MD: major depression.

Article Snippet: Primers for cDNA amplification of HDAC5 (Hs00608366_m1), SIRT2 (Hs01560289_m1), ADRB2 (Hs00240532_s1), BDNF (Hs02718934_s1), KLF2 (Hs00360439_g1), IL-6 (Hs02718934_s1), HDAC2 (Hs00231032_m1), SIRT1 (Hs01009006_m1) and FOXP3 (Hs01085834_m1) were used (Thermo Fisher scientific, MA, USA).

Techniques: Immunofluorescence, Control

Journal: Scientific Reports

Article Title: Epigenetic, neuroplasticity, and adrenergic targets associated with major depression in immune cells

doi: 10.1038/s41598-026-36954-9

Figure Lengend Snippet: Cytoplasm/nucleus ratio of HDAC5 immunofluorescence in monocytes and T-cells of MD patients and HC. Cytoplasm/nucleus ratio of HDAC5 immunofluorescence and regression coefficients (95% CI) in ( A ) classic, intermediate and non-classic monocytes and ( B ) in T-cells of MD and HC. * p < 0.05, ** p < 0.01, *** p < 0.001 as indicated. Differences in ratios among monocyte subsets ( A ) were analysed by two-way ANOVA and in T-cells ( B ) by Student t- test. Abbreviations: HC, healthy controls; MD, major depression; SSRI, selective serotonin reuptake Inhibitor; Double, double action antidepressant; Mod, moderate; Sev, Severe; R, responders; NR, non-responders. ( C ) Statistical correlation (Pearson´s) between MADRS score and HDAC5 ratio in classic, intermediate, non-classic monocytes and T-cells of MD patients.

Article Snippet: Primers for cDNA amplification of HDAC5 (Hs00608366_m1), SIRT2 (Hs01560289_m1), ADRB2 (Hs00240532_s1), BDNF (Hs02718934_s1), KLF2 (Hs00360439_g1), IL-6 (Hs02718934_s1), HDAC2 (Hs00231032_m1), SIRT1 (Hs01009006_m1) and FOXP3 (Hs01085834_m1) were used (Thermo Fisher scientific, MA, USA).

Techniques: Immunofluorescence

Journal: Scientific Reports

Article Title: Epigenetic, neuroplasticity, and adrenergic targets associated with major depression in immune cells

doi: 10.1038/s41598-026-36954-9

Figure Lengend Snippet: HDAC5 mRNA expression is increased in monocytes and T-cells of MD patients. HDAC5 mRNA expression and regression coefficients (95% CI) for HDAC5 mRNA expression in ( A ) classic, ( B ) intermediate and ( C ) non-classic monocytes as well as in (D) T-cells of HC and MD patients. * p < 0.05, ** p < 0.01, *** p < 0.001 as indicated. For MD vs. HC mean comparisons, FDR correction on Student´s t- test was applied.

Article Snippet: Primers for cDNA amplification of HDAC5 (Hs00608366_m1), SIRT2 (Hs01560289_m1), ADRB2 (Hs00240532_s1), BDNF (Hs02718934_s1), KLF2 (Hs00360439_g1), IL-6 (Hs02718934_s1), HDAC2 (Hs00231032_m1), SIRT1 (Hs01009006_m1) and FOXP3 (Hs01085834_m1) were used (Thermo Fisher scientific, MA, USA).

Techniques: Expressing

Journal: Scientific Reports

Article Title: Epigenetic, neuroplasticity, and adrenergic targets associated with major depression in immune cells

doi: 10.1038/s41598-026-36954-9

Figure Lengend Snippet: ADRB2 mRNA expression is increased in monocytes of MD patients and correlate with IL-6 and nuclear enrichment of HDAC5. Gene expression and regression coefficients (95% CI) for ADRB2 mRNA expression in ( A ) classic monocytes and ( B ) T-cells of HC and MD patients. * p < 0.05, ** p < 0.01, *** p < 0.001 as indicated. ( C ) Statistical correlation (Pearson´s) between ADRB2 and IL6 mRNA mRNA expression and HDAC5 ratio in classic monocytes of MD patients. For MD vs. HC mean comparisons, FDR correction on Student´s t- test was applied.

Article Snippet: Primers for cDNA amplification of HDAC5 (Hs00608366_m1), SIRT2 (Hs01560289_m1), ADRB2 (Hs00240532_s1), BDNF (Hs02718934_s1), KLF2 (Hs00360439_g1), IL-6 (Hs02718934_s1), HDAC2 (Hs00231032_m1), SIRT1 (Hs01009006_m1) and FOXP3 (Hs01085834_m1) were used (Thermo Fisher scientific, MA, USA).

Techniques: Expressing, Gene Expression

Journal: Journal of Advanced Research

Article Title: Epigenetically silenced KAT2B suppresses de novo lipogenesis through destroying HDAC5/LSD1 complex assembly in renal cell carcinoma

doi: 10.1016/j.jare.2025.08.007

Figure Lengend Snippet: KAT2B acetylated HDAC5 at K726 B) Venn diagram identifying proteins that interact with KAT2B and potentially regulate lipid metabolism (A). Among the four candidates, HDAC5 has the highest binding affinity with KAT2B (B). (C) Endogenous Co-Immunoprecipitation (Co-IP) experiments identified the interaction between KAT2B and HDAC5 in RCC cells. (D) The exogenous interaction between KAT2B and HDAC5 was determined by Co-IP assays using Flag and Myc antibodies in 293 T cells. (E) Schematic representation of full-length and truncated mutants of the KAT2B-FLAG structure. (F) FLAG-tagged full-length or truncated mutants of KAT2B were expressed in 293 T cells. Extracts were immunoprecipitated with anti-Flag or anti-HDAC5 antibodies, and bound HDAC5 or Flag was examined by western blots using anti-HDAC5 or anti-Flag antibodies. (G) Western blots were used to assess HDAC5 expression and its acetylation levels in RCC cells with KAT2B overexpression. (H) Mass spectra of the K726 site acetylation of HDAC5 after overexpression of KAT2B in 293 T cells. (I) Comparison of K726 and its surrounding residues between different species. (J) Following the overexpression of KAT2B and either wild-type HDAC5 or a K726 site mutant plasmid, the acetylation levels of HDAC5 were assessed. (K) Purified wild-type and acetyltransferase-inactive mutant KAT2B proteins were co-incubated with purified wild-type HDAC5 and K726R mutant proteins in a buffer containing acetyl-CoA. The acetylation level of HDAC5 was analyzed by western blot. (L) Representative fluorescence image of HDAC5 in RCC cells with KAT2B (wild or dead) overexpression and statistical diagram of nuclear and cytoplasmic distribution. (M) The ratio of HDAC5 nuclear fluorescence intensity to cytoplasmic fluorescence intensity in RCC with KAT2B or KAT2B dead overexpression (n = 10). (N) Nuclear HDAC5 expression in RCC cells with KAT2B (wild or dead) overexpression was assessed using western blot. Data were analyzed byone-way ANOVA (M).

Article Snippet: KAT2B overexpression and HDAC5 overexpression lentivirus, KAT2B‐targeted shRNA lentivirus, and overexpression plasmids of LSD1 and KAT2B (wild and enzyme-inactivated) was provided by Genechem Co. Ltd (China).

Techniques: Binding Assay, Immunoprecipitation, Co-Immunoprecipitation Assay, Western Blot, Expressing, Over Expression, Comparison, Mutagenesis, Plasmid Preparation, Purification, Incubation, Fluorescence

Journal: Journal of Advanced Research

Article Title: Epigenetically silenced KAT2B suppresses de novo lipogenesis through destroying HDAC5/LSD1 complex assembly in renal cell carcinoma

doi: 10.1016/j.jare.2025.08.007

Figure Lengend Snippet: KAT2B destroyed HDAC5/LSD1 complex assembly and suppressed FASN transcriptional activity Co-IP assays were performed to verify the interaction strength between wild-type HDAC5 or the K726R mutant and Exportin1 with KAT2B overexpression. (B) Representative immunofluorescence images of wild-type HDAC5, K726R mutant HDAC5, and NES-deleted HDAC5 with KAT2B overexpression in RCC cells. (C-D) Western blots were used to assess HDAC5 and LSD1 expression in RCC cells with KAT2B overexpression or knockdown. (E) The interaction between HDAC5 and LSD1 was determined by Co-IP assays in RCC cells. (F) The interactions between HDAC5 (wild, K726Q, and K726R) and LSD1 were determined by Co-IP assays in 293 T cells. (G) RCC cells were treated with Eltanexor (60 nM) to inhibit Exportin1 activity. The levels of nuclear HDAC5, total HDAC5, Exportin1, and LSD1 were detected using Western blot. (H) Protein stability experiment of LSD1 in RCC cells with KAT2B overexpression after treated with 100 μM cycloheximide (CHX) for 0 h, 1 h, 2 h, 3 h, and 4 h and statistical diagram. (I) Following the addition of chloroquine (10 μM) or MG132 (8 μM) to RCC, LSD1 protein expression was assessed. (J) RCC cells with KAT2B overexpression were immunoprecipitated with LSD1 antibody, and the level of ubiquitin was detected. (K) LSD1 and FASN expression were detected in RCC cells with KAT2B (wild or dead) and/or HDAC5 (wild, 726Q or 726R) overexpression. (L) Schematic diagram illustrating KAT2B-mediated acetylation of HDAC5, promoting its cytoplasmic mislocalization, which resulted in the disruption of the HDAC5-LSD1 complex in the nucleus and subsequent LSD1 degradation.

Article Snippet: KAT2B overexpression and HDAC5 overexpression lentivirus, KAT2B‐targeted shRNA lentivirus, and overexpression plasmids of LSD1 and KAT2B (wild and enzyme-inactivated) was provided by Genechem Co. Ltd (China).

Techniques: Activity Assay, Co-Immunoprecipitation Assay, Mutagenesis, Over Expression, Immunofluorescence, Western Blot, Expressing, Knockdown, Immunoprecipitation, Ubiquitin Proteomics, Disruption

Journal: Journal of Advanced Research

Article Title: Epigenetically silenced KAT2B suppresses de novo lipogenesis through destroying HDAC5/LSD1 complex assembly in renal cell carcinoma

doi: 10.1016/j.jare.2025.08.007

Figure Lengend Snippet: The KAT2B/HDAC5/LSD1/FASN axis repressed RCC lipogenesis and progression in vivo B) The picture of xenografts using Caki-1 cells with KAT2B and/or HDAC5 stable overexpressing. The tumor weight was used for statistical comparison (n = 5). (C) The tumor volume of each group was measured every six days (n = 5). (D) Representative of immunohistochemical (IHC) staining for KAT2B, HDAC5, LSD1, FASN and Ki67 in tumor xenografts. (E) Oil red O staining of the tumor xenografts with KAT2B and/or HDAC5 overexpression. (F) Living fluorescence images of mice in the metastasis model. (G-H) The liver photo and H&E staining of liver tissue in the metastatic model. Data were analyzed by one-way ANOVA (B,C).

Article Snippet: KAT2B overexpression and HDAC5 overexpression lentivirus, KAT2B‐targeted shRNA lentivirus, and overexpression plasmids of LSD1 and KAT2B (wild and enzyme-inactivated) was provided by Genechem Co. Ltd (China).

Techniques: In Vivo, Comparison, Immunohistochemical staining, Immunohistochemistry, Staining, Over Expression, Fluorescence

Journal: Journal of Advanced Research

Article Title: Epigenetically silenced KAT2B suppresses de novo lipogenesis through destroying HDAC5/LSD1 complex assembly in renal cell carcinoma

doi: 10.1016/j.jare.2025.08.007

Figure Lengend Snippet: Graphic abstract of this research TET1-mediated promoter hypermethylation in RCC leaded to decreased KAT2B expression. Mechanistically, KAT2B acetylated HDAC5 at the K726 site and promoted its nucleus export, thereby failing to form a complex with LSD1 in nucleus. This leaded to increased histone methylation levels and decreased FASN expression, ultimately inhibiting lipogenesis and RCC progression. FASN inhibition might be useful in treating KAT2B-low RCC progression by targeting de novo lipogenesis.

Article Snippet: KAT2B overexpression and HDAC5 overexpression lentivirus, KAT2B‐targeted shRNA lentivirus, and overexpression plasmids of LSD1 and KAT2B (wild and enzyme-inactivated) was provided by Genechem Co. Ltd (China).

Techniques: Expressing, Methylation, Inhibition

Journal: bioRxiv

Article Title: HDAC5 -encoded Microprotein NISM Mediates Nucleolar Formation and Ribosomal RNA Synthesis

doi: 10.64898/2026.02.21.707204

Figure Lengend Snippet: (A-B) BedGraph tracks of HEK293T Ribo-seq coverage across the entire HDAC5 transcript (A) and zoomed in on the NISM smORF within the 5′-UTR (B). In (A), the NISM smORF is highlighted in yellow. HDAC5 is on the negative strand and thus the 5′ to 3′ orientation runs right to left. The top tracks show read coverage for cells pre-treated with harringtonine (Harr) to capture translation initiation sites and the bottom tracks show read coverage for untreated cells lysed in the presence of cycloheximide to capture elongating ribosomes. PhyloCSF scores for each reading frame are shown below the RefSeq transcript tracks. Possible start codons in the NISM smORF are denoted by ‘M’ in (B). (C) Sequence alignment showing amino acid level conservation of NISM across distant mammals. (D) Immunoblot analysis of short and long NISM-ALFA expression in HEK293T cells. (E) ESMFold predicted structure of short NISM. Low confidence predictions are colored yellow and very low confidence predictions are colored orange. (F) Representative immunofluorescence images of NPM1 (red), FBL (cyan), and NISM-ALFA (green) in HEK293T cells transfected with empty vector (EV), short NISM-ALFA, or long NISM-ALFA for 48 h. Nuclei were counter-stained with DAPI (blue). Scale bar, 5 µm. All data are representative of at least two biological replicates.

Article Snippet: Expression of HDAC5 at the protein level was also validated by SDS-PAGE and immunoblot using the HDAC5 rabbit monoclonal antibody (Cell Signaling, 20458) following IP of HDAC5 from 500 μg of total protein from WT or NISM KO U2OS cells.

Techniques: Sequencing, Western Blot, Expressing, Immunofluorescence, Transfection, Plasmid Preparation, Staining