human ss18l1 protein sequences Search Results


human anticentromere serum  (Antibodies Inc)
97
Antibodies Inc human anticentromere serum
Human Anticentromere Serum, supplied by Antibodies Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+ss18l1+protein+sequences/Anti-Centromere+Protein+Antibody/pm37516764-243-44-50
Average 97 stars, based on 1 article reviews
human anticentromere serum - by Bioz Stars, 2026-10
97/100 stars
  Buy from Supplier
human anti crest 53 antibodies  (Antibodies Inc)
95
Antibodies Inc human anti crest 53 antibodies
Human Anti Crest 53 Antibodies, supplied by Antibodies Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+ss18l1+protein+sequences/Anti-Centromere+Protein+Antibody/pmc07700014-610-31-36
Average 95 stars, based on 1 article reviews
human anti crest 53 antibodies - by Bioz Stars, 2026-10
95/100 stars
  Buy from Supplier
rabbit anti crest  (Proteintech)
93
Proteintech rabbit anti crest
Rabbit Anti Crest, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+ss18l1+protein+sequences/CREST+Antibody/pm28973294-166-44-46
Average 93 stars, based on 1 article reviews
rabbit anti crest - by Bioz Stars, 2026-10
93/100 stars
  Buy from Supplier
human ss18l1 protein sequences  (Biotechnology Information)
86
Biotechnology Information human ss18l1 protein sequences
Human Ss18l1 Protein Sequences, supplied by Biotechnology Information, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+ss18l1+protein+sequences/arid2+cdna+human+rerepresentative/us12473334-1212-5-23
Average 86 stars, based on 1 article reviews
human ss18l1 protein sequences - by Bioz Stars, 2026-10
86/100 stars
  Buy from Supplier
human iggs against centromere proteins  (Antibodies Inc)
93
Antibodies Inc human iggs against centromere proteins
Human Iggs Against Centromere Proteins, supplied by Antibodies Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+ss18l1+protein+sequences/Anti-Centromere+Protein+Antibody/pmc03318109-213-0-9
Average 93 stars, based on 1 article reviews
human iggs against centromere proteins - by Bioz Stars, 2026-10
93/100 stars
  Buy from Supplier
α ss18  (Cell Signaling Technology Inc)
94
Cell Signaling Technology Inc α ss18
a Schematic of mouse brain soluble nuclear protein extract (NE) preparation, density sedimentation of nuclear proteins over a 10–30% glycerol gradient, and immunoprecipitation of BAF chromatin remodeling complexes. Blue lettering indicates neuronal-specific BAF subunits. Red lettering indicates PBAF-specific subunits. b Density sedimentation of adult Brwd1 FLAG-HA brain NE over a 10–30% glycerol gradient indicates that BRWD1 predominantly associates with large protein complexes. Subunits of BAF and AP-1 complexes serve as molecular weight markers: SMARCA2/4 antibody indicates all BAF complexes including non-canonical GBAF (~1 MDa) , canonical BAF (~2 MDa) and Polybromo-containing BAF (PBAF, ~3 MDa); ACTL6B and SS18L1 indicate neuronal-specific BAF complexes; c-Jun indicates AP-1 (160–440 kDa). HA signal at the expected molecular weight of BRWD1-FLAG-HA (~260 kDa) is observed in fractions containing the BAF complex. c Endogenous BRWD1-FLAG-HA interacts with BAF complexes in embryonic brain. BAF complexes were immunoprecipitated from Brwd1 FLAG-HA brain NE with antibodies against the BAF core ATPase SMARCA4, the neural progenitor subunit <t>SS18,</t> the neuronal subunit SS18L1 or IgG as a control. Endogenous BRWD1-FLAG-HA robustly co-immunoprecipitated with SMARCA4 and the neural progenitor subunit SS18, but less so with the neuronal subunit SS18L1 from E17.5 brain. d BAF complexes purified from adult Brwd1 FLAG-HA brain NE with antibodies against SMARCA4 or the neuronal subunit SS18L1 co-immunoprecipitate BRWD1-FLAG-HA. e The stability of the BAF:BRWD1-FLAG-HA interaction was challenged with increasing concentrations (0.25-4 M) of the denaturing agent, urea. A fraction of BRWD1 remained bound to BAF in up to 4 M urea, surpassing the stability of the dedicated BAF subunit, SMARCB1. f Quantification of urea denaturation experiments, as shown in e , with the amount of bound protein normalized to the amount of immunoprecipitated SMARCA4 ( n = 3 experiments). Source data are provided as a file. See Supplementary Fig. for uncropped blots with MW markers.
α Ss18, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+ss18l1+protein+sequences/SS18+Rabbit+mAb/pmc09606253-372-42-47
Average 94 stars, based on 1 article reviews
α ss18 - by Bioz Stars, 2026-10
94/100 stars
  Buy from Supplier
anticentromere autoimmune serum (crest; human monoclonal)  (Cortex Biochem Inc)
90
Cortex Biochem Inc anticentromere autoimmune serum (crest; human monoclonal)
a Schematic of mouse brain soluble nuclear protein extract (NE) preparation, density sedimentation of nuclear proteins over a 10–30% glycerol gradient, and immunoprecipitation of BAF chromatin remodeling complexes. Blue lettering indicates neuronal-specific BAF subunits. Red lettering indicates PBAF-specific subunits. b Density sedimentation of adult Brwd1 FLAG-HA brain NE over a 10–30% glycerol gradient indicates that BRWD1 predominantly associates with large protein complexes. Subunits of BAF and AP-1 complexes serve as molecular weight markers: SMARCA2/4 antibody indicates all BAF complexes including non-canonical GBAF (~1 MDa) , canonical BAF (~2 MDa) and Polybromo-containing BAF (PBAF, ~3 MDa); ACTL6B and SS18L1 indicate neuronal-specific BAF complexes; c-Jun indicates AP-1 (160–440 kDa). HA signal at the expected molecular weight of BRWD1-FLAG-HA (~260 kDa) is observed in fractions containing the BAF complex. c Endogenous BRWD1-FLAG-HA interacts with BAF complexes in embryonic brain. BAF complexes were immunoprecipitated from Brwd1 FLAG-HA brain NE with antibodies against the BAF core ATPase SMARCA4, the neural progenitor subunit <t>SS18,</t> the neuronal subunit SS18L1 or IgG as a control. Endogenous BRWD1-FLAG-HA robustly co-immunoprecipitated with SMARCA4 and the neural progenitor subunit SS18, but less so with the neuronal subunit SS18L1 from E17.5 brain. d BAF complexes purified from adult Brwd1 FLAG-HA brain NE with antibodies against SMARCA4 or the neuronal subunit SS18L1 co-immunoprecipitate BRWD1-FLAG-HA. e The stability of the BAF:BRWD1-FLAG-HA interaction was challenged with increasing concentrations (0.25-4 M) of the denaturing agent, urea. A fraction of BRWD1 remained bound to BAF in up to 4 M urea, surpassing the stability of the dedicated BAF subunit, SMARCB1. f Quantification of urea denaturation experiments, as shown in e , with the amount of bound protein normalized to the amount of immunoprecipitated SMARCA4 ( n = 3 experiments). Source data are provided as a file. See Supplementary Fig. for uncropped blots with MW markers.
Anticentromere Autoimmune Serum (Crest; Human Monoclonal), supplied by Cortex Biochem Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+ss18l1+protein+sequences/crest+anti+centromere+antibodies/pm17535846-312-80-88
Average 90 stars, based on 1 article reviews
anticentromere autoimmune serum (crest; human monoclonal) - by Bioz Stars, 2026-10
90/100 stars
  Buy from Supplier
anti smarca4  (Cell Signaling Technology Inc)
96
Cell Signaling Technology Inc anti smarca4
a Schematic of mouse brain soluble nuclear protein extract (NE) preparation, density sedimentation of nuclear proteins over a 10–30% glycerol gradient, and immunoprecipitation of BAF chromatin remodeling complexes. Blue lettering indicates neuronal-specific BAF subunits. Red lettering indicates PBAF-specific subunits. b Density sedimentation of adult Brwd1 FLAG-HA brain NE over a 10–30% glycerol gradient indicates that BRWD1 predominantly associates with large protein complexes. Subunits of BAF and AP-1 complexes serve as molecular weight markers: SMARCA2/4 antibody indicates all BAF complexes including non-canonical GBAF (~1 MDa) , canonical BAF (~2 MDa) and Polybromo-containing BAF (PBAF, ~3 MDa); ACTL6B and SS18L1 indicate neuronal-specific BAF complexes; c-Jun indicates AP-1 (160–440 kDa). HA signal at the expected molecular weight of BRWD1-FLAG-HA (~260 kDa) is observed in fractions containing the BAF complex. c Endogenous BRWD1-FLAG-HA interacts with BAF complexes in embryonic brain. BAF complexes were immunoprecipitated from Brwd1 FLAG-HA brain NE with antibodies against the BAF core ATPase SMARCA4, the neural progenitor subunit <t>SS18,</t> the neuronal subunit SS18L1 or IgG as a control. Endogenous BRWD1-FLAG-HA robustly co-immunoprecipitated with SMARCA4 and the neural progenitor subunit SS18, but less so with the neuronal subunit SS18L1 from E17.5 brain. d BAF complexes purified from adult Brwd1 FLAG-HA brain NE with antibodies against SMARCA4 or the neuronal subunit SS18L1 co-immunoprecipitate BRWD1-FLAG-HA. e The stability of the BAF:BRWD1-FLAG-HA interaction was challenged with increasing concentrations (0.25-4 M) of the denaturing agent, urea. A fraction of BRWD1 remained bound to BAF in up to 4 M urea, surpassing the stability of the dedicated BAF subunit, SMARCB1. f Quantification of urea denaturation experiments, as shown in e , with the amount of bound protein normalized to the amount of immunoprecipitated SMARCA4 ( n = 3 experiments). Source data are provided as a file. See Supplementary Fig. for uncropped blots with MW markers.
Anti Smarca4, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+ss18l1+protein+sequences/Brg1+Rabbit+mAb/pmc11544104-269-32-33
Average 96 stars, based on 1 article reviews
anti smarca4 - by Bioz Stars, 2026-10
96/100 stars
  Buy from Supplier
baf250a  (Cell Signaling Technology Inc)
96
Cell Signaling Technology Inc baf250a
a Schematic of mouse brain soluble nuclear protein extract (NE) preparation, density sedimentation of nuclear proteins over a 10–30% glycerol gradient, and immunoprecipitation of BAF chromatin remodeling complexes. Blue lettering indicates neuronal-specific BAF subunits. Red lettering indicates PBAF-specific subunits. b Density sedimentation of adult Brwd1 FLAG-HA brain NE over a 10–30% glycerol gradient indicates that BRWD1 predominantly associates with large protein complexes. Subunits of BAF and AP-1 complexes serve as molecular weight markers: SMARCA2/4 antibody indicates all BAF complexes including non-canonical GBAF (~1 MDa) , canonical BAF (~2 MDa) and Polybromo-containing BAF (PBAF, ~3 MDa); ACTL6B and SS18L1 indicate neuronal-specific BAF complexes; c-Jun indicates AP-1 (160–440 kDa). HA signal at the expected molecular weight of BRWD1-FLAG-HA (~260 kDa) is observed in fractions containing the BAF complex. c Endogenous BRWD1-FLAG-HA interacts with BAF complexes in embryonic brain. BAF complexes were immunoprecipitated from Brwd1 FLAG-HA brain NE with antibodies against the BAF core ATPase SMARCA4, the neural progenitor subunit <t>SS18,</t> the neuronal subunit SS18L1 or IgG as a control. Endogenous BRWD1-FLAG-HA robustly co-immunoprecipitated with SMARCA4 and the neural progenitor subunit SS18, but less so with the neuronal subunit SS18L1 from E17.5 brain. d BAF complexes purified from adult Brwd1 FLAG-HA brain NE with antibodies against SMARCA4 or the neuronal subunit SS18L1 co-immunoprecipitate BRWD1-FLAG-HA. e The stability of the BAF:BRWD1-FLAG-HA interaction was challenged with increasing concentrations (0.25-4 M) of the denaturing agent, urea. A fraction of BRWD1 remained bound to BAF in up to 4 M urea, surpassing the stability of the dedicated BAF subunit, SMARCB1. f Quantification of urea denaturation experiments, as shown in e , with the amount of bound protein normalized to the amount of immunoprecipitated SMARCA4 ( n = 3 experiments). Source data are provided as a file. See Supplementary Fig. for uncropped blots with MW markers.
Baf250a, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+ss18l1+protein+sequences/ARID1A%2FBAF250A+Rabbit+mAb/bio_rxiv__2021__09__15__460446-369-42-44
Average 96 stars, based on 1 article reviews
baf250a - by Bioz Stars, 2026-10
96/100 stars
  Buy from Supplier
brm  (Cell Signaling Technology Inc)
96
Cell Signaling Technology Inc brm
a Schematic of mouse brain soluble nuclear protein extract (NE) preparation, density sedimentation of nuclear proteins over a 10–30% glycerol gradient, and immunoprecipitation of BAF chromatin remodeling complexes. Blue lettering indicates neuronal-specific BAF subunits. Red lettering indicates PBAF-specific subunits. b Density sedimentation of adult Brwd1 FLAG-HA brain NE over a 10–30% glycerol gradient indicates that BRWD1 predominantly associates with large protein complexes. Subunits of BAF and AP-1 complexes serve as molecular weight markers: SMARCA2/4 antibody indicates all BAF complexes including non-canonical GBAF (~1 MDa) , canonical BAF (~2 MDa) and Polybromo-containing BAF (PBAF, ~3 MDa); ACTL6B and SS18L1 indicate neuronal-specific BAF complexes; c-Jun indicates AP-1 (160–440 kDa). HA signal at the expected molecular weight of BRWD1-FLAG-HA (~260 kDa) is observed in fractions containing the BAF complex. c Endogenous BRWD1-FLAG-HA interacts with BAF complexes in embryonic brain. BAF complexes were immunoprecipitated from Brwd1 FLAG-HA brain NE with antibodies against the BAF core ATPase SMARCA4, the neural progenitor subunit <t>SS18,</t> the neuronal subunit SS18L1 or IgG as a control. Endogenous BRWD1-FLAG-HA robustly co-immunoprecipitated with SMARCA4 and the neural progenitor subunit SS18, but less so with the neuronal subunit SS18L1 from E17.5 brain. d BAF complexes purified from adult Brwd1 FLAG-HA brain NE with antibodies against SMARCA4 or the neuronal subunit SS18L1 co-immunoprecipitate BRWD1-FLAG-HA. e The stability of the BAF:BRWD1-FLAG-HA interaction was challenged with increasing concentrations (0.25-4 M) of the denaturing agent, urea. A fraction of BRWD1 remained bound to BAF in up to 4 M urea, surpassing the stability of the dedicated BAF subunit, SMARCB1. f Quantification of urea denaturation experiments, as shown in e , with the amount of bound protein normalized to the amount of immunoprecipitated SMARCA4 ( n = 3 experiments). Source data are provided as a file. See Supplementary Fig. for uncropped blots with MW markers.
Brm, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+ss18l1+protein+sequences/BRM+XP+Rabbit+mAb/bio_rxiv__2021__09__15__460446-369-47-49
Average 96 stars, based on 1 article reviews
brm - by Bioz Stars, 2026-10
96/100 stars
  Buy from Supplier
baf170  (Cell Signaling Technology Inc)
95
Cell Signaling Technology Inc baf170
(A) Purified IPMK and in vitro translated FLAG-SMARCB1 were co-incubated, immunoprecipitated with FLAG antibody, and subjected to immunoblotting. (B) Sf9 insect cells were co-infected with baculoviruses expressing FLAG-IPMK and individual subunits of SWI/SNF complex (SMARCB1, BRG1, BAF155, and <t>BAF170),</t> followed by FLAG M2 agarose immunoprecipitation and immunoblotting. (C) IPMK and IgG were immunoprecipitated from E14Tg2a cells and subjected to immunoblotting. (D) SMARCB1 and IgG were immunoprecipitated from E14Tg2a cells and subjected to immunoblotting. (E) E14Tg2a cells were transfected with FLAG-IPMK or FLAG (a control vector), followed by FLAG immunoprecipitation and immunoblotting. (F) E14Tg2a cells were transfected with siRNA against Egfp ( Egfp KD) and Ipmk ( Ipmk KD), immunoprecipitated with IPMK and IgG, and subjected to immunoblotting.
Baf170, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+ss18l1+protein+sequences/SMARCC2%2FBAF170+Rabbit+mAb/bio_rxiv__2021__09__15__460446-369-37-39
Average 95 stars, based on 1 article reviews
baf170 - by Bioz Stars, 2026-10
95/100 stars
  Buy from Supplier
baf155  (Cell Signaling Technology Inc)
95
Cell Signaling Technology Inc baf155
(A) Purified IPMK and in vitro translated FLAG-SMARCB1 were co-incubated, immunoprecipitated with FLAG antibody, and subjected to immunoblotting. (B) Sf9 insect cells were co-infected with baculoviruses expressing FLAG-IPMK and individual subunits of SWI/SNF complex (SMARCB1, BRG1, <t>BAF155,</t> and BAF170), followed by FLAG M2 agarose immunoprecipitation and immunoblotting. (C) IPMK and IgG were immunoprecipitated from E14Tg2a cells and subjected to immunoblotting. (D) SMARCB1 and IgG were immunoprecipitated from E14Tg2a cells and subjected to immunoblotting. (E) E14Tg2a cells were transfected with FLAG-IPMK or FLAG (a control vector), followed by FLAG immunoprecipitation and immunoblotting. (F) E14Tg2a cells were transfected with siRNA against Egfp ( Egfp KD) and Ipmk ( Ipmk KD), immunoprecipitated with IPMK and IgG, and subjected to immunoblotting.
Baf155, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+ss18l1+protein+sequences/SMARCC1%2FBAF155+Rabbit+mAb/bio_rxiv__2021__09__15__460446-369-32-34
Average 95 stars, based on 1 article reviews
baf155 - by Bioz Stars, 2026-10
95/100 stars
  Buy from Supplier

Image Search Results


a Schematic of mouse brain soluble nuclear protein extract (NE) preparation, density sedimentation of nuclear proteins over a 10–30% glycerol gradient, and immunoprecipitation of BAF chromatin remodeling complexes. Blue lettering indicates neuronal-specific BAF subunits. Red lettering indicates PBAF-specific subunits. b Density sedimentation of adult Brwd1 FLAG-HA brain NE over a 10–30% glycerol gradient indicates that BRWD1 predominantly associates with large protein complexes. Subunits of BAF and AP-1 complexes serve as molecular weight markers: SMARCA2/4 antibody indicates all BAF complexes including non-canonical GBAF (~1 MDa) , canonical BAF (~2 MDa) and Polybromo-containing BAF (PBAF, ~3 MDa); ACTL6B and SS18L1 indicate neuronal-specific BAF complexes; c-Jun indicates AP-1 (160–440 kDa). HA signal at the expected molecular weight of BRWD1-FLAG-HA (~260 kDa) is observed in fractions containing the BAF complex. c Endogenous BRWD1-FLAG-HA interacts with BAF complexes in embryonic brain. BAF complexes were immunoprecipitated from Brwd1 FLAG-HA brain NE with antibodies against the BAF core ATPase SMARCA4, the neural progenitor subunit SS18, the neuronal subunit SS18L1 or IgG as a control. Endogenous BRWD1-FLAG-HA robustly co-immunoprecipitated with SMARCA4 and the neural progenitor subunit SS18, but less so with the neuronal subunit SS18L1 from E17.5 brain. d BAF complexes purified from adult Brwd1 FLAG-HA brain NE with antibodies against SMARCA4 or the neuronal subunit SS18L1 co-immunoprecipitate BRWD1-FLAG-HA. e The stability of the BAF:BRWD1-FLAG-HA interaction was challenged with increasing concentrations (0.25-4 M) of the denaturing agent, urea. A fraction of BRWD1 remained bound to BAF in up to 4 M urea, surpassing the stability of the dedicated BAF subunit, SMARCB1. f Quantification of urea denaturation experiments, as shown in e , with the amount of bound protein normalized to the amount of immunoprecipitated SMARCA4 ( n = 3 experiments). Source data are provided as a file. See Supplementary Fig. for uncropped blots with MW markers.

Journal: Nature Communications

Article Title: Rescue of deficits by Brwd1 copy number restoration in the Ts65Dn mouse model of Down syndrome

doi: 10.1038/s41467-022-34200-0

Figure Lengend Snippet: a Schematic of mouse brain soluble nuclear protein extract (NE) preparation, density sedimentation of nuclear proteins over a 10–30% glycerol gradient, and immunoprecipitation of BAF chromatin remodeling complexes. Blue lettering indicates neuronal-specific BAF subunits. Red lettering indicates PBAF-specific subunits. b Density sedimentation of adult Brwd1 FLAG-HA brain NE over a 10–30% glycerol gradient indicates that BRWD1 predominantly associates with large protein complexes. Subunits of BAF and AP-1 complexes serve as molecular weight markers: SMARCA2/4 antibody indicates all BAF complexes including non-canonical GBAF (~1 MDa) , canonical BAF (~2 MDa) and Polybromo-containing BAF (PBAF, ~3 MDa); ACTL6B and SS18L1 indicate neuronal-specific BAF complexes; c-Jun indicates AP-1 (160–440 kDa). HA signal at the expected molecular weight of BRWD1-FLAG-HA (~260 kDa) is observed in fractions containing the BAF complex. c Endogenous BRWD1-FLAG-HA interacts with BAF complexes in embryonic brain. BAF complexes were immunoprecipitated from Brwd1 FLAG-HA brain NE with antibodies against the BAF core ATPase SMARCA4, the neural progenitor subunit SS18, the neuronal subunit SS18L1 or IgG as a control. Endogenous BRWD1-FLAG-HA robustly co-immunoprecipitated with SMARCA4 and the neural progenitor subunit SS18, but less so with the neuronal subunit SS18L1 from E17.5 brain. d BAF complexes purified from adult Brwd1 FLAG-HA brain NE with antibodies against SMARCA4 or the neuronal subunit SS18L1 co-immunoprecipitate BRWD1-FLAG-HA. e The stability of the BAF:BRWD1-FLAG-HA interaction was challenged with increasing concentrations (0.25-4 M) of the denaturing agent, urea. A fraction of BRWD1 remained bound to BAF in up to 4 M urea, surpassing the stability of the dedicated BAF subunit, SMARCB1. f Quantification of urea denaturation experiments, as shown in e , with the amount of bound protein normalized to the amount of immunoprecipitated SMARCA4 ( n = 3 experiments). Source data are provided as a file. See Supplementary Fig. for uncropped blots with MW markers.

Article Snippet: Antibodies used for immunoprecipitation were: mouse IgG (Santa Cruz cat. # sc-2025), α-SMARCA4 (BRG1 H-10, mouse monoclonal, Santa Cruz cat. # sc-374197), α-SS18L1#1 (CREST M-15, goat polyclonal, Santa Cruz cat. # sc-50912), α-SS18L1#2 (CREST D-7, mouse monoclonal, Santa Cruz cat. # sc-515827), α-SS18 (SS18 D6I4Z, rabbit monoclonal, Cell Signaling cat. # 21792), (α-SMARCC2 (BAF170 E-6, mouse monoclonal, Santa Cruz cat. # sc-17838), α-SMARCB1 (INI1/BAF47 A-5, mouse monocolonal, Santa Cruz cat. # sc-166165), α-SMARCD3 (BAF60C RN-18, mouse monoclonal, Santa Cruz cat. # sc-101163; this antibody did not appear to work for IP).

Techniques: Sedimentation, Immunoprecipitation, Molecular Weight, Control, Purification

(A) Purified IPMK and in vitro translated FLAG-SMARCB1 were co-incubated, immunoprecipitated with FLAG antibody, and subjected to immunoblotting. (B) Sf9 insect cells were co-infected with baculoviruses expressing FLAG-IPMK and individual subunits of SWI/SNF complex (SMARCB1, BRG1, BAF155, and BAF170), followed by FLAG M2 agarose immunoprecipitation and immunoblotting. (C) IPMK and IgG were immunoprecipitated from E14Tg2a cells and subjected to immunoblotting. (D) SMARCB1 and IgG were immunoprecipitated from E14Tg2a cells and subjected to immunoblotting. (E) E14Tg2a cells were transfected with FLAG-IPMK or FLAG (a control vector), followed by FLAG immunoprecipitation and immunoblotting. (F) E14Tg2a cells were transfected with siRNA against Egfp ( Egfp KD) and Ipmk ( Ipmk KD), immunoprecipitated with IPMK and IgG, and subjected to immunoblotting.

Journal: bioRxiv

Article Title: IPMK physically binds to the SWI/SNF complex and modulates BRG1 occupancy

doi: 10.1101/2021.09.15.460446

Figure Lengend Snippet: (A) Purified IPMK and in vitro translated FLAG-SMARCB1 were co-incubated, immunoprecipitated with FLAG antibody, and subjected to immunoblotting. (B) Sf9 insect cells were co-infected with baculoviruses expressing FLAG-IPMK and individual subunits of SWI/SNF complex (SMARCB1, BRG1, BAF155, and BAF170), followed by FLAG M2 agarose immunoprecipitation and immunoblotting. (C) IPMK and IgG were immunoprecipitated from E14Tg2a cells and subjected to immunoblotting. (D) SMARCB1 and IgG were immunoprecipitated from E14Tg2a cells and subjected to immunoblotting. (E) E14Tg2a cells were transfected with FLAG-IPMK or FLAG (a control vector), followed by FLAG immunoprecipitation and immunoblotting. (F) E14Tg2a cells were transfected with siRNA against Egfp ( Egfp KD) and Ipmk ( Ipmk KD), immunoprecipitated with IPMK and IgG, and subjected to immunoblotting.

Article Snippet: Antibodies against FLAG (F1804, Sigma Aldrich), IPMK (custom rabbit polyclonal antibody, raised against a mouse IPMK peptide corresponding to amino acids 295-311 (SKAYSTHTKLYAKKHQS; Covance)) (S. ), SMARCB1 (A301-087, Bethyl), BRG1 (ab110641, Abcam), BAF155 (11956, Cell Signaling Technology), BAF170 (12760, Cell Signaling Technology), BAF250A (12354, Cell Signaling Technology), BRM (11966, Cell Signaling Technology), PBAF/PBRM (A301-591A, Bethyl), a-TUBULIN (T5169, Sigma Aldrich), GST (2622, Cell Signaling Technology), LaminB1 (sc-365214, Santa Cruz Biotech), Histone H3 (homemade), GAPDH (sc-32233, Santa Cruz Biotech), anti-DPF2 (ab128149, Abcam), anti-SMARCE1 (ab137081, Abcam), anti-SS18L1 (ab227535, Abcam), anti-ACTL6A (sc-137062, Santa Cruz Biotech), anti-SMARCD1 (sc-135843, Santa Cruz Biotech), anti-BCL7A (HPA019762, Atlas Antibodies) and anti-ACTB (TA811000, Origene) were used for immunoblotting.

Techniques: Purification, In Vitro, Incubation, Immunoprecipitation, Western Blot, Infection, Expressing, Transfection, Control, Plasmid Preparation

(A) Purified IPMK and in vitro translated FLAG-SMARCB1 were co-incubated, immunoprecipitated with FLAG antibody, and subjected to immunoblotting. (B) Sf9 insect cells were co-infected with baculoviruses expressing FLAG-IPMK and individual subunits of SWI/SNF complex (SMARCB1, BRG1, BAF155, and BAF170), followed by FLAG M2 agarose immunoprecipitation and immunoblotting. (C) IPMK and IgG were immunoprecipitated from E14Tg2a cells and subjected to immunoblotting. (D) SMARCB1 and IgG were immunoprecipitated from E14Tg2a cells and subjected to immunoblotting. (E) E14Tg2a cells were transfected with FLAG-IPMK or FLAG (a control vector), followed by FLAG immunoprecipitation and immunoblotting. (F) E14Tg2a cells were transfected with siRNA against Egfp ( Egfp KD) and Ipmk ( Ipmk KD), immunoprecipitated with IPMK and IgG, and subjected to immunoblotting.

Journal: bioRxiv

Article Title: IPMK physically binds to the SWI/SNF complex and modulates BRG1 occupancy

doi: 10.1101/2021.09.15.460446

Figure Lengend Snippet: (A) Purified IPMK and in vitro translated FLAG-SMARCB1 were co-incubated, immunoprecipitated with FLAG antibody, and subjected to immunoblotting. (B) Sf9 insect cells were co-infected with baculoviruses expressing FLAG-IPMK and individual subunits of SWI/SNF complex (SMARCB1, BRG1, BAF155, and BAF170), followed by FLAG M2 agarose immunoprecipitation and immunoblotting. (C) IPMK and IgG were immunoprecipitated from E14Tg2a cells and subjected to immunoblotting. (D) SMARCB1 and IgG were immunoprecipitated from E14Tg2a cells and subjected to immunoblotting. (E) E14Tg2a cells were transfected with FLAG-IPMK or FLAG (a control vector), followed by FLAG immunoprecipitation and immunoblotting. (F) E14Tg2a cells were transfected with siRNA against Egfp ( Egfp KD) and Ipmk ( Ipmk KD), immunoprecipitated with IPMK and IgG, and subjected to immunoblotting.

Article Snippet: Antibodies against FLAG (F1804, Sigma Aldrich), IPMK (custom rabbit polyclonal antibody, raised against a mouse IPMK peptide corresponding to amino acids 295-311 (SKAYSTHTKLYAKKHQS; Covance)) (S. ), SMARCB1 (A301-087, Bethyl), BRG1 (ab110641, Abcam), BAF155 (11956, Cell Signaling Technology), BAF170 (12760, Cell Signaling Technology), BAF250A (12354, Cell Signaling Technology), BRM (11966, Cell Signaling Technology), PBAF/PBRM (A301-591A, Bethyl), a-TUBULIN (T5169, Sigma Aldrich), GST (2622, Cell Signaling Technology), LaminB1 (sc-365214, Santa Cruz Biotech), Histone H3 (homemade), GAPDH (sc-32233, Santa Cruz Biotech), anti-DPF2 (ab128149, Abcam), anti-SMARCE1 (ab137081, Abcam), anti-SS18L1 (ab227535, Abcam), anti-ACTL6A (sc-137062, Santa Cruz Biotech), anti-SMARCD1 (sc-135843, Santa Cruz Biotech), anti-BCL7A (HPA019762, Atlas Antibodies) and anti-ACTB (TA811000, Origene) were used for immunoblotting.

Techniques: Purification, In Vitro, Incubation, Immunoprecipitation, Western Blot, Infection, Expressing, Transfection, Control, Plasmid Preparation

(A) A model displaying the physical interactions between IPMK and SMARCB1 (left). For these physical interactions, the exons 3, 4, and 6 of IPMK (orange boxes) and the Rpt1 and Rpt2 (particularly N-terminal β sheets) domains of SMARCB1 (red boxes) are required. An additional model showing our speculation on position of IPMK within the SWI/SNF complex, directly interacting with SMARCB1, BRG1, and BAF155 (right). (B) In WT mESC (left), IPMK regulates appropriate BRG1 localization (probably via physical interaction with various subunits of SWI/SNF complex) and chromatin accessibility at NFR (nucleosome free region) of TSS. Upon Ipmk depletion (right), BRG1 localization is perturbed, resulting in decreased chromatin accessibility at NFR of TSS.

Journal: bioRxiv

Article Title: IPMK physically binds to the SWI/SNF complex and modulates BRG1 occupancy

doi: 10.1101/2021.09.15.460446

Figure Lengend Snippet: (A) A model displaying the physical interactions between IPMK and SMARCB1 (left). For these physical interactions, the exons 3, 4, and 6 of IPMK (orange boxes) and the Rpt1 and Rpt2 (particularly N-terminal β sheets) domains of SMARCB1 (red boxes) are required. An additional model showing our speculation on position of IPMK within the SWI/SNF complex, directly interacting with SMARCB1, BRG1, and BAF155 (right). (B) In WT mESC (left), IPMK regulates appropriate BRG1 localization (probably via physical interaction with various subunits of SWI/SNF complex) and chromatin accessibility at NFR (nucleosome free region) of TSS. Upon Ipmk depletion (right), BRG1 localization is perturbed, resulting in decreased chromatin accessibility at NFR of TSS.

Article Snippet: Antibodies against FLAG (F1804, Sigma Aldrich), IPMK (custom rabbit polyclonal antibody, raised against a mouse IPMK peptide corresponding to amino acids 295-311 (SKAYSTHTKLYAKKHQS; Covance)) (S. ), SMARCB1 (A301-087, Bethyl), BRG1 (ab110641, Abcam), BAF155 (11956, Cell Signaling Technology), BAF170 (12760, Cell Signaling Technology), BAF250A (12354, Cell Signaling Technology), BRM (11966, Cell Signaling Technology), PBAF/PBRM (A301-591A, Bethyl), a-TUBULIN (T5169, Sigma Aldrich), GST (2622, Cell Signaling Technology), LaminB1 (sc-365214, Santa Cruz Biotech), Histone H3 (homemade), GAPDH (sc-32233, Santa Cruz Biotech), anti-DPF2 (ab128149, Abcam), anti-SMARCE1 (ab137081, Abcam), anti-SS18L1 (ab227535, Abcam), anti-ACTL6A (sc-137062, Santa Cruz Biotech), anti-SMARCD1 (sc-135843, Santa Cruz Biotech), anti-BCL7A (HPA019762, Atlas Antibodies) and anti-ACTB (TA811000, Origene) were used for immunoblotting.

Techniques: