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Proteintech znf410
Summary of pomalidomide- and lenalidomide-derivative compound screen for HbF inducers in HUDEP-2 cells and unbiased global proteomic follow-up. For screening, cells were treated at stages 1 and 2 and collected at stage 3 (see ). ( A ) Pomalidomide (Poma) treatment (1 µM, 6 days) in HUDEP-2 cells induces a 4-fold increase of %HbF + cells as quantified by flow cytometry (p < 0.0001, two-sided t-test). ( B ) A total of 19 compounds induced HbF levels to at least 50% of the internal pomalidomide positive control, as quantified by flow cytometry. Compounds discussed in text are highlighted in color. Compounds 1088 (4-carbon linker), 1089 (5-carbon linker) and 1091 (7-carbon linker) share chemical structure similarity with 1090 , which contains a 6-carbon linker (Supplementary Table S4). ( C ) Direct targets of pomalidomide in HUDEP-2 cells (indicated by asterisks) include known targets IKZF1 and FAM83F and novel targets FBXO22, RASSF5, CDIP1, and KCTD15 (Supplementary Table S6). ( D ) Compound 1075 led to specific degradation of IKZF1 and ZFP91. ( E ) Compound 1090 led to degradation of a subset of major pomalidomide targets, with increased specificity for ZFP91 and CYP2R1. ( F ) Compound 1126 led to degradation of a subset of pomalidomide targets with increased specificity for CYP2R1 and ZPF91 and decreased specificity for IKZF1. ( G ) Compound 1235 , a derivative of lenalidomide, led to degradation of the known lenalidomide targets (indicated by asterisks) IKZF1, CSNK1A1, and FAM83F, along with the novel targets CYP2R1, FIZ1, CDIP1, DAGLB, and ENTPD5. Two proteins (in red labels) were increased: GTF2H3 (FC = 1.67, adjusted p = 0.0022) and NFYA (FC = 2.27, adjusted p = 0.035). NFYA is necessary for hematopoietic stem cell proliferation . ( H ) Western blot of HUDEP-2 cells at stage 2 treated for 6 hours confirms degradation of IKZF1, shows no detectable degradation of BCL11A, and verifies the presence of <t>ZNF410,</t> which was not detected in the mass spectrometry (Supplementary Table S5). FC = fold change. AdjP = adjusted p-value.
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1) Product Images from "Regulation of BCL11A DNA binding and expression in human erythrocyte precursor HUDEP-2 cells"

Article Title: Regulation of BCL11A DNA binding and expression in human erythrocyte precursor HUDEP-2 cells

Journal: bioRxiv

doi: 10.64898/2026.02.06.704516

Summary of pomalidomide- and lenalidomide-derivative compound screen for HbF inducers in HUDEP-2 cells and unbiased global proteomic follow-up. For screening, cells were treated at stages 1 and 2 and collected at stage 3 (see ). ( A ) Pomalidomide (Poma) treatment (1 µM, 6 days) in HUDEP-2 cells induces a 4-fold increase of %HbF + cells as quantified by flow cytometry (p < 0.0001, two-sided t-test). ( B ) A total of 19 compounds induced HbF levels to at least 50% of the internal pomalidomide positive control, as quantified by flow cytometry. Compounds discussed in text are highlighted in color. Compounds 1088 (4-carbon linker), 1089 (5-carbon linker) and 1091 (7-carbon linker) share chemical structure similarity with 1090 , which contains a 6-carbon linker (Supplementary Table S4). ( C ) Direct targets of pomalidomide in HUDEP-2 cells (indicated by asterisks) include known targets IKZF1 and FAM83F and novel targets FBXO22, RASSF5, CDIP1, and KCTD15 (Supplementary Table S6). ( D ) Compound 1075 led to specific degradation of IKZF1 and ZFP91. ( E ) Compound 1090 led to degradation of a subset of major pomalidomide targets, with increased specificity for ZFP91 and CYP2R1. ( F ) Compound 1126 led to degradation of a subset of pomalidomide targets with increased specificity for CYP2R1 and ZPF91 and decreased specificity for IKZF1. ( G ) Compound 1235 , a derivative of lenalidomide, led to degradation of the known lenalidomide targets (indicated by asterisks) IKZF1, CSNK1A1, and FAM83F, along with the novel targets CYP2R1, FIZ1, CDIP1, DAGLB, and ENTPD5. Two proteins (in red labels) were increased: GTF2H3 (FC = 1.67, adjusted p = 0.0022) and NFYA (FC = 2.27, adjusted p = 0.035). NFYA is necessary for hematopoietic stem cell proliferation . ( H ) Western blot of HUDEP-2 cells at stage 2 treated for 6 hours confirms degradation of IKZF1, shows no detectable degradation of BCL11A, and verifies the presence of ZNF410, which was not detected in the mass spectrometry (Supplementary Table S5). FC = fold change. AdjP = adjusted p-value.
Figure Legend Snippet: Summary of pomalidomide- and lenalidomide-derivative compound screen for HbF inducers in HUDEP-2 cells and unbiased global proteomic follow-up. For screening, cells were treated at stages 1 and 2 and collected at stage 3 (see ). ( A ) Pomalidomide (Poma) treatment (1 µM, 6 days) in HUDEP-2 cells induces a 4-fold increase of %HbF + cells as quantified by flow cytometry (p < 0.0001, two-sided t-test). ( B ) A total of 19 compounds induced HbF levels to at least 50% of the internal pomalidomide positive control, as quantified by flow cytometry. Compounds discussed in text are highlighted in color. Compounds 1088 (4-carbon linker), 1089 (5-carbon linker) and 1091 (7-carbon linker) share chemical structure similarity with 1090 , which contains a 6-carbon linker (Supplementary Table S4). ( C ) Direct targets of pomalidomide in HUDEP-2 cells (indicated by asterisks) include known targets IKZF1 and FAM83F and novel targets FBXO22, RASSF5, CDIP1, and KCTD15 (Supplementary Table S6). ( D ) Compound 1075 led to specific degradation of IKZF1 and ZFP91. ( E ) Compound 1090 led to degradation of a subset of major pomalidomide targets, with increased specificity for ZFP91 and CYP2R1. ( F ) Compound 1126 led to degradation of a subset of pomalidomide targets with increased specificity for CYP2R1 and ZPF91 and decreased specificity for IKZF1. ( G ) Compound 1235 , a derivative of lenalidomide, led to degradation of the known lenalidomide targets (indicated by asterisks) IKZF1, CSNK1A1, and FAM83F, along with the novel targets CYP2R1, FIZ1, CDIP1, DAGLB, and ENTPD5. Two proteins (in red labels) were increased: GTF2H3 (FC = 1.67, adjusted p = 0.0022) and NFYA (FC = 2.27, adjusted p = 0.035). NFYA is necessary for hematopoietic stem cell proliferation . ( H ) Western blot of HUDEP-2 cells at stage 2 treated for 6 hours confirms degradation of IKZF1, shows no detectable degradation of BCL11A, and verifies the presence of ZNF410, which was not detected in the mass spectrometry (Supplementary Table S5). FC = fold change. AdjP = adjusted p-value.

Techniques Used: Flow Cytometry, Positive Control, Western Blot, Mass Spectrometry

Models of BCL11A regulation across three complementary layers. ( A ) The ZF0-mediated oligomerization assembles different BCL11A splice variants (depicted as different lengths), all of which contain ZF0, enabling BCL11A to form high-order polymers. ( B ) The EED inhibitor FTX6058 reduces BCL11A dosage mainly through LIN28B, which modulates BCL11A translation. ( C ) Sequence alignment of known pomalidomide degrons (IKZF1 and ZFP91) and dWIZ-2 target (WIZ), and the corresponding ZF units of ZNF410 and BCL11A. Zinc-coordinating residues are colored blue, and residues critical for the selectivity of pomalidomide- or lenalidomide-derived degraders are shown in red. ( D ) The pomalidomide-derived compound 1075 induces degradation of ZFP91 and IKZF1, reshaping the regulatory network contributing to HbF induction.
Figure Legend Snippet: Models of BCL11A regulation across three complementary layers. ( A ) The ZF0-mediated oligomerization assembles different BCL11A splice variants (depicted as different lengths), all of which contain ZF0, enabling BCL11A to form high-order polymers. ( B ) The EED inhibitor FTX6058 reduces BCL11A dosage mainly through LIN28B, which modulates BCL11A translation. ( C ) Sequence alignment of known pomalidomide degrons (IKZF1 and ZFP91) and dWIZ-2 target (WIZ), and the corresponding ZF units of ZNF410 and BCL11A. Zinc-coordinating residues are colored blue, and residues critical for the selectivity of pomalidomide- or lenalidomide-derived degraders are shown in red. ( D ) The pomalidomide-derived compound 1075 induces degradation of ZFP91 and IKZF1, reshaping the regulatory network contributing to HbF induction.

Techniques Used: Sequencing, Derivative Assay

Related Articles

Expressing:

Article Title: ZNF410 represses fetal globin by singular control of CHD4.
Article Snippet: .. Nuclear extracts from CD34+ HSPC-derived erythroblasts on day 11 of erythroid maturation culture were used to assess ZNF410 (Proteintech, 14529-1-AP), CHD4 (Abcam, ab70469), GATAD2A (Bethyl Laboratories, A302-358A), MTA2 (Abcam, ab8106), MBD2 (Bethyl Laboratories, A301-632A), HDAC2 (Abcam, ab32117), RBBP4 (Bethyl Laboratories, A301-206A-T) and GAPDH (Cell Signaling Technology, 5174S) protein expression. ..

Chromatin Immunoprecipitation:

Article Title: ZNF410 Uniquely Activates the NuRD Component CHD4 to Silence Fetal Hemoglobin Expression
Article Snippet: .. ZNF410 (Proteintech, Cat. # 14529-1-AP), HA (Sigma, Cat. # 11815016001) and H3K27ac (Abcam, Cat. # ab4729) antibodies were used for ChIP. ..

Article Title: ZNF410 uniquely activates the NuRD component CHD4 to silence fetal hemoglobin expression
Article Snippet: .. ZNF410 (Proteintech, Cat. # 14529-1-AP), HA (Sigma, Cat. # 11815016001) and H3K27ac (Abcam, Cat. # ab4729) antibodies were used for ChIP. ..

Western Blot:

Article Title: ZNF410 uniquely activates the NuRD component CHD4 to silence fetal hemoglobin expression
Article Snippet: .. Western blotting analysis was carried out according to standard protocol with the following antibodies: ZNF410 (1:500, Proteintech, Cat. # 14529-1-AP), CHD4 (1:500, Proteintech, Cat. # 14173-1-AP), CHD4 (1:500, Cell Signaling Cat. # 11912S), GATAD2A (1;1000, Bethyl Laboratories, Cat. # A302-358A-T), HDAC2 (1;1000, Bethyl Laboratories, Cat. # A300-705A-T), MBD2 (1;1000, Bethyl Laboratories, Cat. # A301-633A-T), MTA2 (1;1000, Bethyl Laboratories, Cat. # A300-395A-T), HA (1:1000, Cell Signaling Cat. #3724), FLAG (1:1000, Sigma, Cat. # F1804), BCL11A (1:1000, Abcam, Cat. #19487), LRF (1:1000, eBioscience Cat. #13E9), GATA1 (1:1000, Santa Cruz, Cat. #sc-265), γ-globin (1:1000, Santa Cruz, Cat. #sc-21756), β-actin (1:1000, Santa-Cruz, Cat. #sc-47778). .. Secondary antibodies: anti-rabbit (1:10,000, GE Healthcare, Cat. #NA934V); anti-mouse (1:10,000, GE Healthcare, Cat. #NA931V) anti-Rat (1: 5,000, ThermoFisher Scientific, Cat. #31470), anti-Hamster (1: 5,000, ThermoFisher Scientific, Cat. # PA1-32045).



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Summary of pomalidomide- and lenalidomide-derivative compound screen for HbF inducers in HUDEP-2 cells and unbiased global proteomic follow-up. For screening, cells were treated at stages 1 and 2 and collected at stage 3 (see ). ( A ) Pomalidomide (Poma) treatment (1 µM, 6 days) in HUDEP-2 cells induces a 4-fold increase of %HbF + cells as quantified by flow cytometry (p < 0.0001, two-sided t-test). ( B ) A total of 19 compounds induced HbF levels to at least 50% of the internal pomalidomide positive control, as quantified by flow cytometry. Compounds discussed in text are highlighted in color. Compounds 1088 (4-carbon linker), 1089 (5-carbon linker) and 1091 (7-carbon linker) share chemical structure similarity with 1090 , which contains a 6-carbon linker (Supplementary Table S4). ( C ) Direct targets of pomalidomide in HUDEP-2 cells (indicated by asterisks) include known targets IKZF1 and FAM83F and novel targets FBXO22, RASSF5, CDIP1, and KCTD15 (Supplementary Table S6). ( D ) Compound 1075 led to specific degradation of IKZF1 and ZFP91. ( E ) Compound 1090 led to degradation of a subset of major pomalidomide targets, with increased specificity for ZFP91 and CYP2R1. ( F ) Compound 1126 led to degradation of a subset of pomalidomide targets with increased specificity for CYP2R1 and ZPF91 and decreased specificity for IKZF1. ( G ) Compound 1235 , a derivative of lenalidomide, led to degradation of the known lenalidomide targets (indicated by asterisks) IKZF1, CSNK1A1, and FAM83F, along with the novel targets CYP2R1, FIZ1, CDIP1, DAGLB, and ENTPD5. Two proteins (in red labels) were increased: GTF2H3 (FC = 1.67, adjusted p = 0.0022) and NFYA (FC = 2.27, adjusted p = 0.035). NFYA is necessary for hematopoietic stem cell proliferation . ( H ) Western blot of HUDEP-2 cells at stage 2 treated for 6 hours confirms degradation of IKZF1, shows no detectable degradation of BCL11A, and verifies the presence of <t>ZNF410,</t> which was not detected in the mass spectrometry (Supplementary Table S5). FC = fold change. AdjP = adjusted p-value.
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Image Search Results


Summary of pomalidomide- and lenalidomide-derivative compound screen for HbF inducers in HUDEP-2 cells and unbiased global proteomic follow-up. For screening, cells were treated at stages 1 and 2 and collected at stage 3 (see ). ( A ) Pomalidomide (Poma) treatment (1 µM, 6 days) in HUDEP-2 cells induces a 4-fold increase of %HbF + cells as quantified by flow cytometry (p < 0.0001, two-sided t-test). ( B ) A total of 19 compounds induced HbF levels to at least 50% of the internal pomalidomide positive control, as quantified by flow cytometry. Compounds discussed in text are highlighted in color. Compounds 1088 (4-carbon linker), 1089 (5-carbon linker) and 1091 (7-carbon linker) share chemical structure similarity with 1090 , which contains a 6-carbon linker (Supplementary Table S4). ( C ) Direct targets of pomalidomide in HUDEP-2 cells (indicated by asterisks) include known targets IKZF1 and FAM83F and novel targets FBXO22, RASSF5, CDIP1, and KCTD15 (Supplementary Table S6). ( D ) Compound 1075 led to specific degradation of IKZF1 and ZFP91. ( E ) Compound 1090 led to degradation of a subset of major pomalidomide targets, with increased specificity for ZFP91 and CYP2R1. ( F ) Compound 1126 led to degradation of a subset of pomalidomide targets with increased specificity for CYP2R1 and ZPF91 and decreased specificity for IKZF1. ( G ) Compound 1235 , a derivative of lenalidomide, led to degradation of the known lenalidomide targets (indicated by asterisks) IKZF1, CSNK1A1, and FAM83F, along with the novel targets CYP2R1, FIZ1, CDIP1, DAGLB, and ENTPD5. Two proteins (in red labels) were increased: GTF2H3 (FC = 1.67, adjusted p = 0.0022) and NFYA (FC = 2.27, adjusted p = 0.035). NFYA is necessary for hematopoietic stem cell proliferation . ( H ) Western blot of HUDEP-2 cells at stage 2 treated for 6 hours confirms degradation of IKZF1, shows no detectable degradation of BCL11A, and verifies the presence of ZNF410, which was not detected in the mass spectrometry (Supplementary Table S5). FC = fold change. AdjP = adjusted p-value.

Journal: bioRxiv

Article Title: Regulation of BCL11A DNA binding and expression in human erythrocyte precursor HUDEP-2 cells

doi: 10.64898/2026.02.06.704516

Figure Lengend Snippet: Summary of pomalidomide- and lenalidomide-derivative compound screen for HbF inducers in HUDEP-2 cells and unbiased global proteomic follow-up. For screening, cells were treated at stages 1 and 2 and collected at stage 3 (see ). ( A ) Pomalidomide (Poma) treatment (1 µM, 6 days) in HUDEP-2 cells induces a 4-fold increase of %HbF + cells as quantified by flow cytometry (p < 0.0001, two-sided t-test). ( B ) A total of 19 compounds induced HbF levels to at least 50% of the internal pomalidomide positive control, as quantified by flow cytometry. Compounds discussed in text are highlighted in color. Compounds 1088 (4-carbon linker), 1089 (5-carbon linker) and 1091 (7-carbon linker) share chemical structure similarity with 1090 , which contains a 6-carbon linker (Supplementary Table S4). ( C ) Direct targets of pomalidomide in HUDEP-2 cells (indicated by asterisks) include known targets IKZF1 and FAM83F and novel targets FBXO22, RASSF5, CDIP1, and KCTD15 (Supplementary Table S6). ( D ) Compound 1075 led to specific degradation of IKZF1 and ZFP91. ( E ) Compound 1090 led to degradation of a subset of major pomalidomide targets, with increased specificity for ZFP91 and CYP2R1. ( F ) Compound 1126 led to degradation of a subset of pomalidomide targets with increased specificity for CYP2R1 and ZPF91 and decreased specificity for IKZF1. ( G ) Compound 1235 , a derivative of lenalidomide, led to degradation of the known lenalidomide targets (indicated by asterisks) IKZF1, CSNK1A1, and FAM83F, along with the novel targets CYP2R1, FIZ1, CDIP1, DAGLB, and ENTPD5. Two proteins (in red labels) were increased: GTF2H3 (FC = 1.67, adjusted p = 0.0022) and NFYA (FC = 2.27, adjusted p = 0.035). NFYA is necessary for hematopoietic stem cell proliferation . ( H ) Western blot of HUDEP-2 cells at stage 2 treated for 6 hours confirms degradation of IKZF1, shows no detectable degradation of BCL11A, and verifies the presence of ZNF410, which was not detected in the mass spectrometry (Supplementary Table S5). FC = fold change. AdjP = adjusted p-value.

Article Snippet: Primary antibodies included DNMT1 (Cell Signaling Technology - CST #5032), H3K9me2 (CST #4658), H3K27me3 (CST #9733s), H3 (CST #14269), EED (CST #51673), GAPDH (CST #5174), β-globin (37-8) (Santa Cruz #21757), γ-globin (51-7) (Santa Cruz #21756), BCL11A (Novus Biologicals #NB600-261), ZNF410 (Proteintech #14529-1-AP), IKZF1 (CST #14859) and actin (Sigma-Aldrich #A2228).

Techniques: Flow Cytometry, Positive Control, Western Blot, Mass Spectrometry

Models of BCL11A regulation across three complementary layers. ( A ) The ZF0-mediated oligomerization assembles different BCL11A splice variants (depicted as different lengths), all of which contain ZF0, enabling BCL11A to form high-order polymers. ( B ) The EED inhibitor FTX6058 reduces BCL11A dosage mainly through LIN28B, which modulates BCL11A translation. ( C ) Sequence alignment of known pomalidomide degrons (IKZF1 and ZFP91) and dWIZ-2 target (WIZ), and the corresponding ZF units of ZNF410 and BCL11A. Zinc-coordinating residues are colored blue, and residues critical for the selectivity of pomalidomide- or lenalidomide-derived degraders are shown in red. ( D ) The pomalidomide-derived compound 1075 induces degradation of ZFP91 and IKZF1, reshaping the regulatory network contributing to HbF induction.

Journal: bioRxiv

Article Title: Regulation of BCL11A DNA binding and expression in human erythrocyte precursor HUDEP-2 cells

doi: 10.64898/2026.02.06.704516

Figure Lengend Snippet: Models of BCL11A regulation across three complementary layers. ( A ) The ZF0-mediated oligomerization assembles different BCL11A splice variants (depicted as different lengths), all of which contain ZF0, enabling BCL11A to form high-order polymers. ( B ) The EED inhibitor FTX6058 reduces BCL11A dosage mainly through LIN28B, which modulates BCL11A translation. ( C ) Sequence alignment of known pomalidomide degrons (IKZF1 and ZFP91) and dWIZ-2 target (WIZ), and the corresponding ZF units of ZNF410 and BCL11A. Zinc-coordinating residues are colored blue, and residues critical for the selectivity of pomalidomide- or lenalidomide-derived degraders are shown in red. ( D ) The pomalidomide-derived compound 1075 induces degradation of ZFP91 and IKZF1, reshaping the regulatory network contributing to HbF induction.

Article Snippet: Primary antibodies included DNMT1 (Cell Signaling Technology - CST #5032), H3K9me2 (CST #4658), H3K27me3 (CST #9733s), H3 (CST #14269), EED (CST #51673), GAPDH (CST #5174), β-globin (37-8) (Santa Cruz #21757), γ-globin (51-7) (Santa Cruz #21756), BCL11A (Novus Biologicals #NB600-261), ZNF410 (Proteintech #14529-1-AP), IKZF1 (CST #14859) and actin (Sigma-Aldrich #A2228).

Techniques: Sequencing, Derivative Assay

Figure 7. The N terminus of ZNF410 enables SWI/SNF complex recruitment (A) Schematic representation of the construction for truncated forms of HA-TurboID-ZNF410. (B) Validation of the streptavidin IP of truncated forms of HA-TurboID-ZNF410 associating with SMARCA2 or SMARCA4. The ratios of SMARCA2 or SMARCA4 to HA-tagged bait protein were quantified using ImageJ software.

Journal: Cell reports

Article Title: SWI/SNF complex-mediated ZNF410 cooperative binding maintains chromatin accessibility and enhancer activity.

doi: 10.1016/j.celrep.2025.115476

Figure Lengend Snippet: Figure 7. The N terminus of ZNF410 enables SWI/SNF complex recruitment (A) Schematic representation of the construction for truncated forms of HA-TurboID-ZNF410. (B) Validation of the streptavidin IP of truncated forms of HA-TurboID-ZNF410 associating with SMARCA2 or SMARCA4. The ratios of SMARCA2 or SMARCA4 to HA-tagged bait protein were quantified using ImageJ software.

Article Snippet: After removal of the insoluble debris, the cell lysate was pre-cleared with 50 mL Protein A/G agarose beads for 2 h at 4 C. Taking 4% of precleared chromatin set aside as input and the remainder was added Protein A/G beads pre-bound with specific antibodies against ZNF410 (Proteintech, 14529-1-AP), H3K27ac (Abcam, ab4729), H3K4me3 (Abcam, ab8580) and H3K9me3 (Abcam, ab8898) overnight.

Techniques: Biomarker Discovery, Software

Figure 7. The N terminus of ZNF410 enables SWI/SNF complex recruitment (A) Schematic representation of the construction for truncated forms of HA-TurboID-ZNF410. (B) Validation of the streptavidin IP of truncated forms of HA-TurboID-ZNF410 associating with SMARCA2 or SMARCA4. The ratios of SMARCA2 or SMARCA4 to HA-tagged bait protein were quantified using ImageJ software.

Journal: Cell reports

Article Title: SWI/SNF complex-mediated ZNF410 cooperative binding maintains chromatin accessibility and enhancer activity.

doi: 10.1016/j.celrep.2025.115476

Figure Lengend Snippet: Figure 7. The N terminus of ZNF410 enables SWI/SNF complex recruitment (A) Schematic representation of the construction for truncated forms of HA-TurboID-ZNF410. (B) Validation of the streptavidin IP of truncated forms of HA-TurboID-ZNF410 associating with SMARCA2 or SMARCA4. The ratios of SMARCA2 or SMARCA4 to HA-tagged bait protein were quantified using ImageJ software.

Article Snippet: REAGENT or RESOURCE SOURCE IDENTIFIER Antibodies Rabbit Anti-ZNF410 Polyclonal Antibody Proteintech Cat#:14529-1-AP; RRID:AB_2257520 Rabbit Anti-SMARCA2 Polyclonal Antibody Proteintech Cat#:26613-1-AP; RRID: AB_2880575 Rabbit Anti-SMARCA4 Polyclonal Antibody Proteintech Cat#:21634-1-AP; RRID: AB_10858784 Rabbit H3K27ac Polyclonal Antibody Abcam Cat#:ab4729; RRID:AB_2118291 Rabbit H3K4me3 Polyclonal Antibody Abcam Cat#:ab8580; RRID:AB_306649 Rabbit H3K9me3 Polyclonal Antibody Abcam Cat#:ab8898; RRID:AB_306848 Hemoglobin Gamma (51-7) Antibody Santa Cruz Biotechnology Cat#:sc-21756; RRID:AB_2295004 Rabbit HA-Tag Antibody Cell Signaling Technology Cat#:#3724; RRID:AB_1549585 Beta-Actin Polyclonal Antibody Proteintech Cat#:20536-1-AP; RRID:AB_10700003 HRP-conjugated Streptavidin Proteintech Cat#: SA00001-0 Goat Anti-Mouse IgG (H + L), Secondary Antibody, HRP Proteintech Cat#:SA00001-1; RRID:AB_2722565 Goat Anti-Rabbit IgG (H + L), Secondary Antibody, HRP Proteintech Cat#:SA00001-2; RRID:AB_2722564 Bacterial and virus strains Stbl3TM Thermo Fisher Scientific Cat#:C737303 Chemicals, peptides, and recombinant proteins Hexadimethrine bromide (polybrene) Sigma-Aldrich H9268 Polyethylenimine, Linear, MW 25,000 (PEI 25000) Polysciences 23966–1 Puromycin dihydrochloride Sigma-Aldrich P8833 Biotin Sigma-Aldrich B4501 PierceTM Streptavidin Magnetic Beads Thermo Fisher Scientific 88816 Agencourt AMPure XP Beckman Coulter A63880 Dynabeads Protein A Thermo Fisher Scientific 10002D Dynabeads Protein G Thermo Fisher Scientific 10004D 16% Formaldehyde Thermo Fisher Scientific 28908 Glycine Thermo Fisher Scientific BP381-1 Proteinase K Thermo Fisher Scientific 25530049 RNase A Thermo Fisher Scientific EN0531 T4 DNA polymerase New England Biolabs M0203L HiFi DNA Assembly Master Mix New England Biolabs E2621L Phusion Flash High-Fidelity PCR Master Mix Thermo Fisher Scientific F548S HiScript II 1st Strand cDNA Synthesis Kit Vazyme R212 FastStart SYBR Green Master Mix Roche 4913914001 Penicillin/Streptomycin Thermo Fisher Scientific 15140122 Recombinant Human SCF Peprotech 300–07 Epoetin Alfa AMGEN 55513-144-10 Critical commercial assays MinElute Gel Extraction Kit QIAGEN 28604 QIAquick PCR Purification Kit QIAGEN 28104 QIAprep Spin Miniprep Kit QIAGEN 27106 RNeasy Mini Kit QIAGEN 74104 (Continued on next page) 18 Cell Reports 44, 115476, April 22, 2025

Techniques: Biomarker Discovery, Software