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1 6 hexanediol  (TargetMol)


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    Structured Review

    TargetMol 1 6 hexanediol
    1 6 Hexanediol, supplied by TargetMol, used in various techniques. Bioz Stars score: 94/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/1 6 hexanediol/product/TargetMol
    Average 94 stars, based on 6 article reviews
    1 6 hexanediol - by Bioz Stars, 2026-02
    94/100 stars

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    Figure 1. GATA3 undergoes PS in cells and in vitro (A) Confocal microscopy images of HEK293T cells expressing GATA3WT-mEGFP (green). Nuclei were stained with DAPI (purple). Scale bar, 5 μm. (B) Line-scan intensity profiles of GATA3WT-mEGFP and DAPI signals along the yellow arrow in (A). (C) Time-lapse snapshots of fluorescence recovery after photobleaching (FRAP) in HEK293T cells expressing GATA3WT-mEGFP. Scale bar, 2 μm. (D) FRAP recovery kinetics of GATA3WT-mEGFP condensates (n = 3). t1/2, half-recovery time. (E) Representative snapshots of HEK293T expressing GATA3WT-mEGFP <t>with</t> <t>5%</t> <t>1,6-hexanediol</t> treatment across the indicated time. Scale bar, 2 μm. (F) Representative images of 10 μM purified MBP-GATA3WT protein solution in tubes and under microscope with or without TEV protease treatment. Scale bar, 20 μm.
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    Figure 1. GATA3 undergoes PS in cells and in vitro (A) Confocal microscopy images of HEK293T cells expressing GATA3WT-mEGFP (green). Nuclei were stained with DAPI (purple). Scale bar, 5 μm. (B) Line-scan intensity profiles of GATA3WT-mEGFP and DAPI signals along the yellow arrow in (A). (C) Time-lapse snapshots of fluorescence recovery after photobleaching (FRAP) in HEK293T cells expressing GATA3WT-mEGFP. Scale bar, 2 μm. (D) FRAP recovery kinetics of GATA3WT-mEGFP condensates (n = 3). t1/2, half-recovery time. (E) Representative snapshots of HEK293T expressing GATA3WT-mEGFP <t>with</t> <t>5%</t> <t>1,6-hexanediol</t> treatment across the indicated time. Scale bar, 2 μm. (F) Representative images of 10 μM purified MBP-GATA3WT protein solution in tubes and under microscope with or without TEV protease treatment. Scale bar, 20 μm.
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    Figure 1. GATA3 undergoes PS in cells and in vitro (A) Confocal microscopy images of HEK293T cells expressing GATA3WT-mEGFP (green). Nuclei were stained with DAPI (purple). Scale bar, 5 μm. (B) Line-scan intensity profiles of GATA3WT-mEGFP and DAPI signals along the yellow arrow in (A). (C) Time-lapse snapshots of fluorescence recovery after photobleaching (FRAP) in HEK293T cells expressing GATA3WT-mEGFP. Scale bar, 2 μm. (D) FRAP recovery kinetics of GATA3WT-mEGFP condensates (n = 3). t1/2, half-recovery time. (E) Representative snapshots of HEK293T expressing GATA3WT-mEGFP <t>with</t> <t>5%</t> <t>1,6-hexanediol</t> treatment across the indicated time. Scale bar, 2 μm. (F) Representative images of 10 μM purified MBP-GATA3WT protein solution in tubes and under microscope with or without TEV protease treatment. Scale bar, 20 μm.
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    Figure 1. GATA3 undergoes PS in cells and in vitro (A) Confocal microscopy images of HEK293T cells expressing GATA3WT-mEGFP (green). Nuclei were stained with DAPI (purple). Scale bar, 5 μm. (B) Line-scan intensity profiles of GATA3WT-mEGFP and DAPI signals along the yellow arrow in (A). (C) Time-lapse snapshots of fluorescence recovery after photobleaching (FRAP) in HEK293T cells expressing GATA3WT-mEGFP. Scale bar, 2 μm. (D) FRAP recovery kinetics of GATA3WT-mEGFP condensates (n = 3). t1/2, half-recovery time. (E) Representative snapshots of HEK293T expressing GATA3WT-mEGFP <t>with</t> <t>5%</t> <t>1,6-hexanediol</t> treatment across the indicated time. Scale bar, 2 μm. (F) Representative images of 10 μM purified MBP-GATA3WT protein solution in tubes and under microscope with or without TEV protease treatment. Scale bar, 20 μm.
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    EB1 selectively forms coacervates with TIP150 and MCAK. ( A and B ) Schematic representations of the domain structures (upper) and sequence features (lower) of human TIP150 ( A ) and MCAK ( B ). TIP150-CT (aa 800–1368), containing the EBD and the C-coil domain, was used in this study. The line at 0.5 (y-axis) is the cut-off for disorder (>0.5) and order (<0.5) predictions. The VLXT predictor was used for disordered dispositions. ( C ) Representative micrographs showing enrichment of TIP150-CT and/or MCAK in EB1 droplets in BRB80 buffer. All protein concentrations were 20 μM. All groups are displayed using identical fluorescence image settings. TIP150-CT, TIP150-CT-mCherry; MCAK, MCAK-mCherry; T+M, TIP150-CT-mCherry + MCAK-mCherry. Hex, <t>1,6-hexanediol.</t> Scale bar, 10 μm. ( D ) Statistical analyses of the droplet area shown in C ( n = 560 droplets for each group). Data are presented as mean ± standard error of the mean (SEM) ( n = 3 bilogical repeats) and were examined by one-way analysis of variance (ANOVA) with Tukey's multiple comparisons test. P -values are indicated. NS, not significant. ( E ) FRAP analysis of co-droplets formed by TIP150-CT and/or MCAK with EB1 (time shown as min:sec). All protein concentrations were 20 μM. Scale bar, 5 μm. ( F ) Quantitative analyses of the fluorescence inside the droplet over time shown in E . Data are presented as mean ± SEM at each time point ( n = 6 droplets combined from three independent repeats).
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    Figure 1. GATA3 undergoes PS in cells and in vitro (A) Confocal microscopy images of HEK293T cells expressing GATA3WT-mEGFP (green). Nuclei were stained with DAPI (purple). Scale bar, 5 μm. (B) Line-scan intensity profiles of GATA3WT-mEGFP and DAPI signals along the yellow arrow in (A). (C) Time-lapse snapshots of fluorescence recovery after photobleaching (FRAP) in HEK293T cells expressing GATA3WT-mEGFP. Scale bar, 2 μm. (D) FRAP recovery kinetics of GATA3WT-mEGFP condensates (n = 3). t1/2, half-recovery time. (E) Representative snapshots of HEK293T expressing GATA3WT-mEGFP with 5% 1,6-hexanediol treatment across the indicated time. Scale bar, 2 μm. (F) Representative images of 10 μM purified MBP-GATA3WT protein solution in tubes and under microscope with or without TEV protease treatment. Scale bar, 20 μm.

    Journal: Cell reports

    Article Title: GATA3 differentially regulates the transcriptome via zinc finger 2-modulated phase separation.

    doi: 10.1016/j.celrep.2025.115702

    Figure Lengend Snippet: Figure 1. GATA3 undergoes PS in cells and in vitro (A) Confocal microscopy images of HEK293T cells expressing GATA3WT-mEGFP (green). Nuclei were stained with DAPI (purple). Scale bar, 5 μm. (B) Line-scan intensity profiles of GATA3WT-mEGFP and DAPI signals along the yellow arrow in (A). (C) Time-lapse snapshots of fluorescence recovery after photobleaching (FRAP) in HEK293T cells expressing GATA3WT-mEGFP. Scale bar, 2 μm. (D) FRAP recovery kinetics of GATA3WT-mEGFP condensates (n = 3). t1/2, half-recovery time. (E) Representative snapshots of HEK293T expressing GATA3WT-mEGFP with 5% 1,6-hexanediol treatment across the indicated time. Scale bar, 2 μm. (F) Representative images of 10 μM purified MBP-GATA3WT protein solution in tubes and under microscope with or without TEV protease treatment. Scale bar, 20 μm.

    Article Snippet: REAGENT or RESOURCE SOURCE IDENTIFIER Antibodies GATA3 abcam Cat# ab199428 GAPDH abcam Cat# ab8245 H3K27ac abcam Cat# ab4729 H3K9me3 abcam Cat# ab8898 H3 abcam Cat# ab1791 suv39H1 abcam Cat# ab283262 Anti-RNA polymerase II (phospho S2) abcam Cat# ab193468 Anti-KAT3B / p300 abcam Cat# ab275378 Rabbit polyclonal to GFP abcam Cat# ab290 Rig-I/DDX58 Rabbit mAb ABclonal Cat# A22478 IRF-3 Rabbit mAb Cell Signaling Technology Cat# 4302 Phospho-IRF-3 (Ser386) Rabbit mAb Cell Signaling Technology Cat# 37829 Phospho-IRF-3 (Ser396) Rabbit mAb Cell Signaling Technology Cat# 4947 HA-Tag Rabbit mAb ABclonal Cat# AE105 TBK1/NAK Rabbit mAb ABclonal Cat# A3458 Donkey anti-goat IgG-HRP abcam Cat# ab6885 Phospho-TBK1/NAK (Ser172) Rabbit mAb Cell Signaling Technology Cat# 5483 Anti-KMT1E/SETDB1 abcam Cat# ab300573 Estrogen Receptor alpha Santa Cruz Cat# sc-73562 PML Santa Cruz Cat# sc-71910 Anti-SC35 abcam Cat# ab204916 Mouse monoclonal [IH10] to Coilin abcam Cat# ab87913 Bacterial and virus strains E. coli DH5α Lab stored N/A E. coli BL21/DE3 Lab stored N/A Lentivirus Lab stored N/A Chemicals, peptides, and recombinant proteins IPTG Sigma-Aldrich Cat# I6758 PMSF Sigma-Aldrich Cat# 329-98-6 LipofectamineTM 2000 Thermo Fisher Scientific Cat# 11668027 Puromycin Sigma-Aldrich Cat# 540222 Chaetocin MCE Cat# 28097-03-2 5-Azacytidine MCE Cat# 320-67-2 β-Estradiol MCE Cat# 50-28-2 Cycloheximide MCE Cat# 66-81-9 1,6-Hexanediol aladdin Cat# 629-11-8 X-tremeGENETM HP DNA Sigma-Aldrich Cat# 6366244001 Recombinant MBP-GATA3-WT protein This study N/A Recombinant MBP-GATA3-N protein This study N/A Recombinant MBP-GATA3-C protein This study N/A Recombinant MBP-GATA3-DBD protein This study N/A Recombinant MBP-GATA3-ΔN protein This study N/A Recombinant MBP-GATA3-ΔC protein This study N/A (Continued on next page) 18 Cell Reports 44, 115702, May 27, 2025

    Techniques: In Vitro, Confocal Microscopy, Expressing, Staining, Fluorescence, Purification, Microscopy

    Figure 3. Positively charged amino acids of ZnF2 modulate GATA3 condensate formation (A) Representative images of droplet formation of 5 μM GATA3WT-mEGFP in the presence of 10% 1,6-hexanediol (1,6-Hex). (B) Turbidity measurements of GATA3WT-mEGFP solutions with and without 10% 1,6-Hex treatment. Data are presented as means ±SD. ***p < 0.001. (C) Representative images of GATA3WT-mEGFP droplets at increasing NaCl concentrations ranging from 37.5 to 300 mM, as indicated. Scale bar, 5 μm. (D) Quantification of droplet area corresponding to (C). Data are presented as means ± SD. **p < 0.01 and ***p < 0.001. (E) Net charge distribution analysis of the GATA3 protein sequence. Red indicates negatively charged residues; blue indicates positively charged residues. The DBD region is highlighted in orange. Lysine (K) and arginine (R) residues within the DBD are specifically marked in blue font. (F) Representative images of HEK293T cells expressing GATA3WT-mEGFP and its mutants, as indicated. Scale bar, 5 μm. (G) Quantification of the number of condensates in HEK293T cells expressing GATA3WT-mEGFP and its mutants. Data are presented as means ± SD. *p < 0.05 and ***p < 0.001. (H) Representative snapshots from FRAP assays in HEK293T cells expressing GATA3WT-mEGFP or its mutants, as indicated. Scale bar, 2 μm. (I) Quantitative analysis of the average fluorescence recovery of GATA3WT-mEGFP condensates and their mutants (n = 3), as shown in (H).

    Journal: Cell reports

    Article Title: GATA3 differentially regulates the transcriptome via zinc finger 2-modulated phase separation.

    doi: 10.1016/j.celrep.2025.115702

    Figure Lengend Snippet: Figure 3. Positively charged amino acids of ZnF2 modulate GATA3 condensate formation (A) Representative images of droplet formation of 5 μM GATA3WT-mEGFP in the presence of 10% 1,6-hexanediol (1,6-Hex). (B) Turbidity measurements of GATA3WT-mEGFP solutions with and without 10% 1,6-Hex treatment. Data are presented as means ±SD. ***p < 0.001. (C) Representative images of GATA3WT-mEGFP droplets at increasing NaCl concentrations ranging from 37.5 to 300 mM, as indicated. Scale bar, 5 μm. (D) Quantification of droplet area corresponding to (C). Data are presented as means ± SD. **p < 0.01 and ***p < 0.001. (E) Net charge distribution analysis of the GATA3 protein sequence. Red indicates negatively charged residues; blue indicates positively charged residues. The DBD region is highlighted in orange. Lysine (K) and arginine (R) residues within the DBD are specifically marked in blue font. (F) Representative images of HEK293T cells expressing GATA3WT-mEGFP and its mutants, as indicated. Scale bar, 5 μm. (G) Quantification of the number of condensates in HEK293T cells expressing GATA3WT-mEGFP and its mutants. Data are presented as means ± SD. *p < 0.05 and ***p < 0.001. (H) Representative snapshots from FRAP assays in HEK293T cells expressing GATA3WT-mEGFP or its mutants, as indicated. Scale bar, 2 μm. (I) Quantitative analysis of the average fluorescence recovery of GATA3WT-mEGFP condensates and their mutants (n = 3), as shown in (H).

    Article Snippet: REAGENT or RESOURCE SOURCE IDENTIFIER Antibodies GATA3 abcam Cat# ab199428 GAPDH abcam Cat# ab8245 H3K27ac abcam Cat# ab4729 H3K9me3 abcam Cat# ab8898 H3 abcam Cat# ab1791 suv39H1 abcam Cat# ab283262 Anti-RNA polymerase II (phospho S2) abcam Cat# ab193468 Anti-KAT3B / p300 abcam Cat# ab275378 Rabbit polyclonal to GFP abcam Cat# ab290 Rig-I/DDX58 Rabbit mAb ABclonal Cat# A22478 IRF-3 Rabbit mAb Cell Signaling Technology Cat# 4302 Phospho-IRF-3 (Ser386) Rabbit mAb Cell Signaling Technology Cat# 37829 Phospho-IRF-3 (Ser396) Rabbit mAb Cell Signaling Technology Cat# 4947 HA-Tag Rabbit mAb ABclonal Cat# AE105 TBK1/NAK Rabbit mAb ABclonal Cat# A3458 Donkey anti-goat IgG-HRP abcam Cat# ab6885 Phospho-TBK1/NAK (Ser172) Rabbit mAb Cell Signaling Technology Cat# 5483 Anti-KMT1E/SETDB1 abcam Cat# ab300573 Estrogen Receptor alpha Santa Cruz Cat# sc-73562 PML Santa Cruz Cat# sc-71910 Anti-SC35 abcam Cat# ab204916 Mouse monoclonal [IH10] to Coilin abcam Cat# ab87913 Bacterial and virus strains E. coli DH5α Lab stored N/A E. coli BL21/DE3 Lab stored N/A Lentivirus Lab stored N/A Chemicals, peptides, and recombinant proteins IPTG Sigma-Aldrich Cat# I6758 PMSF Sigma-Aldrich Cat# 329-98-6 LipofectamineTM 2000 Thermo Fisher Scientific Cat# 11668027 Puromycin Sigma-Aldrich Cat# 540222 Chaetocin MCE Cat# 28097-03-2 5-Azacytidine MCE Cat# 320-67-2 β-Estradiol MCE Cat# 50-28-2 Cycloheximide MCE Cat# 66-81-9 1,6-Hexanediol aladdin Cat# 629-11-8 X-tremeGENETM HP DNA Sigma-Aldrich Cat# 6366244001 Recombinant MBP-GATA3-WT protein This study N/A Recombinant MBP-GATA3-N protein This study N/A Recombinant MBP-GATA3-C protein This study N/A Recombinant MBP-GATA3-DBD protein This study N/A Recombinant MBP-GATA3-ΔN protein This study N/A Recombinant MBP-GATA3-ΔC protein This study N/A (Continued on next page) 18 Cell Reports 44, 115702, May 27, 2025

    Techniques: Sequencing, Expressing, Fluorescence

    EB1 selectively forms coacervates with TIP150 and MCAK. ( A and B ) Schematic representations of the domain structures (upper) and sequence features (lower) of human TIP150 ( A ) and MCAK ( B ). TIP150-CT (aa 800–1368), containing the EBD and the C-coil domain, was used in this study. The line at 0.5 (y-axis) is the cut-off for disorder (>0.5) and order (<0.5) predictions. The VLXT predictor was used for disordered dispositions. ( C ) Representative micrographs showing enrichment of TIP150-CT and/or MCAK in EB1 droplets in BRB80 buffer. All protein concentrations were 20 μM. All groups are displayed using identical fluorescence image settings. TIP150-CT, TIP150-CT-mCherry; MCAK, MCAK-mCherry; T+M, TIP150-CT-mCherry + MCAK-mCherry. Hex, 1,6-hexanediol. Scale bar, 10 μm. ( D ) Statistical analyses of the droplet area shown in C ( n = 560 droplets for each group). Data are presented as mean ± standard error of the mean (SEM) ( n = 3 bilogical repeats) and were examined by one-way analysis of variance (ANOVA) with Tukey's multiple comparisons test. P -values are indicated. NS, not significant. ( E ) FRAP analysis of co-droplets formed by TIP150-CT and/or MCAK with EB1 (time shown as min:sec). All protein concentrations were 20 μM. Scale bar, 5 μm. ( F ) Quantitative analyses of the fluorescence inside the droplet over time shown in E . Data are presented as mean ± SEM at each time point ( n = 6 droplets combined from three independent repeats).

    Journal: Journal of Molecular Cell Biology

    Article Title: Organization of microtubule plus-end dynamics by phase separation in mitosis

    doi: 10.1093/jmcb/mjae006

    Figure Lengend Snippet: EB1 selectively forms coacervates with TIP150 and MCAK. ( A and B ) Schematic representations of the domain structures (upper) and sequence features (lower) of human TIP150 ( A ) and MCAK ( B ). TIP150-CT (aa 800–1368), containing the EBD and the C-coil domain, was used in this study. The line at 0.5 (y-axis) is the cut-off for disorder (>0.5) and order (<0.5) predictions. The VLXT predictor was used for disordered dispositions. ( C ) Representative micrographs showing enrichment of TIP150-CT and/or MCAK in EB1 droplets in BRB80 buffer. All protein concentrations were 20 μM. All groups are displayed using identical fluorescence image settings. TIP150-CT, TIP150-CT-mCherry; MCAK, MCAK-mCherry; T+M, TIP150-CT-mCherry + MCAK-mCherry. Hex, 1,6-hexanediol. Scale bar, 10 μm. ( D ) Statistical analyses of the droplet area shown in C ( n = 560 droplets for each group). Data are presented as mean ± standard error of the mean (SEM) ( n = 3 bilogical repeats) and were examined by one-way analysis of variance (ANOVA) with Tukey's multiple comparisons test. P -values are indicated. NS, not significant. ( E ) FRAP analysis of co-droplets formed by TIP150-CT and/or MCAK with EB1 (time shown as min:sec). All protein concentrations were 20 μM. Scale bar, 5 μm. ( F ) Quantitative analyses of the fluorescence inside the droplet over time shown in E . Data are presented as mean ± SEM at each time point ( n = 6 droplets combined from three independent repeats).

    Article Snippet: The following chemicals were used: PEG-8000 (Sangon Biotech, A600433) and 1, 6-hexanediol (Sigma, 88571).

    Techniques: Sequencing, Fluorescence