human anti sumo1 Search Results


86
Abcam human sumo 1
A) Representative confocal micrographs showing the nuclear and cytoplasmatic expression of human POLR2E and <t>SUMO-1</t> proteins in vivo, in kidney sections of cisplatin-AKI (AKI-CIS) mice treated or not with MVs and sacrificed 48 hours later, and in vitro by TECs treated with cisplatin and cultured in the absence (vehicle) or in the presence of 50 µg of MVs (MV) for 24 hours. Nuclei were counterstained with Hoechst dye. Original magnification: ×400 for kidney sections and ×630 for TECs. B) 1×10 5 TECs treated with cisplatin and cultured in the absence (CIS) or in the presence of two different preparations of MVs (+MV) for 1 hour were analysed by RT-PCR for specific human mRNA POLR2E . Bands of PCR products specific for human POLR2E of the expected size (90 pb) were detected in a 4% agarose gel electrophoresis. As positive control the extract of human bone marrow-derived MSCs (BM-MSC) was used. The * indicates the control without cDNA.
Human Sumo 1, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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86
Santa Cruz Biotechnology human sumo 1
A) Representative confocal micrographs showing the nuclear and cytoplasmatic expression of human POLR2E and <t>SUMO-1</t> proteins in vivo, in kidney sections of cisplatin-AKI (AKI-CIS) mice treated or not with MVs and sacrificed 48 hours later, and in vitro by TECs treated with cisplatin and cultured in the absence (vehicle) or in the presence of 50 µg of MVs (MV) for 24 hours. Nuclei were counterstained with Hoechst dye. Original magnification: ×400 for kidney sections and ×630 for TECs. B) 1×10 5 TECs treated with cisplatin and cultured in the absence (CIS) or in the presence of two different preparations of MVs (+MV) for 1 hour were analysed by RT-PCR for specific human mRNA POLR2E . Bands of PCR products specific for human POLR2E of the expected size (90 pb) were detected in a 4% agarose gel electrophoresis. As positive control the extract of human bone marrow-derived MSCs (BM-MSC) was used. The * indicates the control without cDNA.
Human Sumo 1, supplied by Santa Cruz Biotechnology, 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/result/human sumo 1/product/Santa Cruz Biotechnology
Average 86 stars, based on 1 article reviews
human sumo 1 - by Bioz Stars, 2025-02
86/100 stars
  Buy from Supplier

86
Santa Cruz Biotechnology human sumo1
A) Representative confocal micrographs showing the nuclear and cytoplasmatic expression of human POLR2E and <t>SUMO-1</t> proteins in vivo, in kidney sections of cisplatin-AKI (AKI-CIS) mice treated or not with MVs and sacrificed 48 hours later, and in vitro by TECs treated with cisplatin and cultured in the absence (vehicle) or in the presence of 50 µg of MVs (MV) for 24 hours. Nuclei were counterstained with Hoechst dye. Original magnification: ×400 for kidney sections and ×630 for TECs. B) 1×10 5 TECs treated with cisplatin and cultured in the absence (CIS) or in the presence of two different preparations of MVs (+MV) for 1 hour were analysed by RT-PCR for specific human mRNA POLR2E . Bands of PCR products specific for human POLR2E of the expected size (90 pb) were detected in a 4% agarose gel electrophoresis. As positive control the extract of human bone marrow-derived MSCs (BM-MSC) was used. The * indicates the control without cDNA.
Human Sumo1, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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human sumo1 - by Bioz Stars, 2025-02
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86
WuXi AppTec anti human sumo1
Real-time RT-PCR and Western blots for <t>SUMO1</t> with and without SUMO1 siRNA transfection in fibroblasts . Three SSc fibroblast strains (two with anti-topo I and one with anti-RNA polymerase III positive serum) were transfected with SUMO1 siRNA. After 48-hour transfection, total RNAs were used for measuring SUMO1 transcript levels (Figure 4a), and the nuclear extracts were used for measuring SUMO1 protein (Figure 4b). Error bars indicate standard deviation.
Anti Human Sumo1, supplied by WuXi AppTec, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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86
Cell Signaling Technology Inc human anti sumo1
Therapeutic benefit of Pml induction by IFNα or poly(I:C) through NEK1 t clearance in vivo . A) NEK1 t modification by <t>SUMO1</t> and SUMO2/3. HEK293 cells were transfected with the indicated expression vectors and treated or not with IFNα. IP: immuno-precipitation, WCL: whole cell lysate. B) IFNα treatment induces proteasome-dependent degradation of NEK1 t in HEK293 cells. MG132: proteasome inhibitor, n=3. C) PML silencing impedes IFNα-induced NEK1 t degradation. Quantifications (right), n=3. D) Western blot of NEK1 t protein from the spinal cord of age-matched Nek1 t/t or Nek1 t/t Pml −/− mice following IFNα or poly(I:C) therapy, (*) non-specific band. E) IFNα or poly(I:C) therapy eliminates NEK1 t aggregates in αMNs of Nek1 t/t mice. Quantifications: ≥30 αMNs from ≥3 mice F) IFNα or poly(I:C) therapies selectively extend lifespan in Pml -proficient Nek1 t/t mice. Arrowhead: therapy initiation, continued until death. G) IFNα or poly(I:C) therapies improve muscle strength and neuromuscular function selectively in Pml -proficient Nek1 t/t ALS mice. Trendlines in Supplementary Fig.S2E.
Human Anti Sumo1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


A) Representative confocal micrographs showing the nuclear and cytoplasmatic expression of human POLR2E and SUMO-1 proteins in vivo, in kidney sections of cisplatin-AKI (AKI-CIS) mice treated or not with MVs and sacrificed 48 hours later, and in vitro by TECs treated with cisplatin and cultured in the absence (vehicle) or in the presence of 50 µg of MVs (MV) for 24 hours. Nuclei were counterstained with Hoechst dye. Original magnification: ×400 for kidney sections and ×630 for TECs. B) 1×10 5 TECs treated with cisplatin and cultured in the absence (CIS) or in the presence of two different preparations of MVs (+MV) for 1 hour were analysed by RT-PCR for specific human mRNA POLR2E . Bands of PCR products specific for human POLR2E of the expected size (90 pb) were detected in a 4% agarose gel electrophoresis. As positive control the extract of human bone marrow-derived MSCs (BM-MSC) was used. The * indicates the control without cDNA.

Journal: PLoS ONE

Article Title: Microvesicles Derived from Mesenchymal Stem Cells Enhance Survival in a Lethal Model of Acute Kidney Injury

doi: 10.1371/journal.pone.0033115

Figure Lengend Snippet: A) Representative confocal micrographs showing the nuclear and cytoplasmatic expression of human POLR2E and SUMO-1 proteins in vivo, in kidney sections of cisplatin-AKI (AKI-CIS) mice treated or not with MVs and sacrificed 48 hours later, and in vitro by TECs treated with cisplatin and cultured in the absence (vehicle) or in the presence of 50 µg of MVs (MV) for 24 hours. Nuclei were counterstained with Hoechst dye. Original magnification: ×400 for kidney sections and ×630 for TECs. B) 1×10 5 TECs treated with cisplatin and cultured in the absence (CIS) or in the presence of two different preparations of MVs (+MV) for 1 hour were analysed by RT-PCR for specific human mRNA POLR2E . Bands of PCR products specific for human POLR2E of the expected size (90 pb) were detected in a 4% agarose gel electrophoresis. As positive control the extract of human bone marrow-derived MSCs (BM-MSC) was used. The * indicates the control without cDNA.

Article Snippet: The following antibodies were used: rabbit anti-human POLR2E (Abcam) and rabbit anti human SUMO-1 (Abcam).

Techniques: Expressing, In Vivo, In Vitro, Cell Culture, Reverse Transcription Polymerase Chain Reaction, Agarose Gel Electrophoresis, Positive Control, Derivative Assay

A) Representative MV size analyses by direct measurement with NTA, showing no difference among MVs treated or not with RNase. B) Representative Bioanalyzer profile, showing the size distribution of total RNA extracted from MVs treated or not with RNAse. The first peak (left side of each panel) represents an internal standard. The two peaks in Sample 1 (black arrows) represent 18 S (left) and 28 S (right) ribosomal RNA, only partially detectable in MVs. The red arrows showed the reduction of 18 and 28 S fragment inside RNAse-treated MVs. C) Histogram showing the expression level of SUMO-1 , POLR2 and Act B transcripts in MVs treated or not with RNase, express as 2 -δCt , as described in material and methods.

Journal: PLoS ONE

Article Title: Microvesicles Derived from Mesenchymal Stem Cells Enhance Survival in a Lethal Model of Acute Kidney Injury

doi: 10.1371/journal.pone.0033115

Figure Lengend Snippet: A) Representative MV size analyses by direct measurement with NTA, showing no difference among MVs treated or not with RNase. B) Representative Bioanalyzer profile, showing the size distribution of total RNA extracted from MVs treated or not with RNAse. The first peak (left side of each panel) represents an internal standard. The two peaks in Sample 1 (black arrows) represent 18 S (left) and 28 S (right) ribosomal RNA, only partially detectable in MVs. The red arrows showed the reduction of 18 and 28 S fragment inside RNAse-treated MVs. C) Histogram showing the expression level of SUMO-1 , POLR2 and Act B transcripts in MVs treated or not with RNase, express as 2 -δCt , as described in material and methods.

Article Snippet: The following antibodies were used: rabbit anti-human POLR2E (Abcam) and rabbit anti human SUMO-1 (Abcam).

Techniques: Expressing

Real-time RT-PCR and Western blots for SUMO1 with and without SUMO1 siRNA transfection in fibroblasts . Three SSc fibroblast strains (two with anti-topo I and one with anti-RNA polymerase III positive serum) were transfected with SUMO1 siRNA. After 48-hour transfection, total RNAs were used for measuring SUMO1 transcript levels (Figure 4a), and the nuclear extracts were used for measuring SUMO1 protein (Figure 4b). Error bars indicate standard deviation.

Journal: Arthritis Research & Therapy

Article Title: Decreased catalytic function with altered sumoylation of DNA topoisomerase I in the nuclei of scleroderma fibroblasts

doi: 10.1186/ar3435

Figure Lengend Snippet: Real-time RT-PCR and Western blots for SUMO1 with and without SUMO1 siRNA transfection in fibroblasts . Three SSc fibroblast strains (two with anti-topo I and one with anti-RNA polymerase III positive serum) were transfected with SUMO1 siRNA. After 48-hour transfection, total RNAs were used for measuring SUMO1 transcript levels (Figure 4a), and the nuclear extracts were used for measuring SUMO1 protein (Figure 4b). Error bars indicate standard deviation.

Article Snippet: Resolved proteins were transferred onto nitrocellulose membranes and incubated with 1:1,000 diluted primary antibodies including mouse anti-human topo I (ImmunoVision, Springdale, AR, USA), anti-human SUMO1 (ABGENT, San Diego, CA, USA) and anti-collagen type I, individually.

Techniques: Quantitative RT-PCR, Western Blot, Transfection, Standard Deviation

Catalytic function of topo I in cultured SSc fibroblasts with and without SUMO1 siRNA transfection . A serial dilution of the nuclear extract containing topo I obtained from SSc fibroblasts was used to relax 0.25 μg supercoiled DNA. In this figure, the supercoiled DNA band was completely transformed to relaxed DNA at dilutions of one half and one in the fibroblasts without siRNA transfection or non-target siRNA transfection. In contrast, this change was observed between the one-eighth and one-fourth dilutions in the fibroblasts with SUMO1 transfection, which indicates a higher efficiency of catalytic function of topo I after SUMO1 inhibition in the fibroblasts. According to the intensity of the bands of remaining supercoiled DNA in serial dilutions in the assays of three fibroblast strains, these changes are significant. The P- values are 0.045 and 0.027 at the one-fourth dilution for comparisons between SUMO1 siRNA vs. non-target siRNA, or vs. without siRNA transfected fibroblasts, respectively (Student's t -test). This is representative of three SSc fibroblast strains examined in SUMO1 siRNA studies. * A , supercoiled DNA; B , relaxed DNA.

Journal: Arthritis Research & Therapy

Article Title: Decreased catalytic function with altered sumoylation of DNA topoisomerase I in the nuclei of scleroderma fibroblasts

doi: 10.1186/ar3435

Figure Lengend Snippet: Catalytic function of topo I in cultured SSc fibroblasts with and without SUMO1 siRNA transfection . A serial dilution of the nuclear extract containing topo I obtained from SSc fibroblasts was used to relax 0.25 μg supercoiled DNA. In this figure, the supercoiled DNA band was completely transformed to relaxed DNA at dilutions of one half and one in the fibroblasts without siRNA transfection or non-target siRNA transfection. In contrast, this change was observed between the one-eighth and one-fourth dilutions in the fibroblasts with SUMO1 transfection, which indicates a higher efficiency of catalytic function of topo I after SUMO1 inhibition in the fibroblasts. According to the intensity of the bands of remaining supercoiled DNA in serial dilutions in the assays of three fibroblast strains, these changes are significant. The P- values are 0.045 and 0.027 at the one-fourth dilution for comparisons between SUMO1 siRNA vs. non-target siRNA, or vs. without siRNA transfected fibroblasts, respectively (Student's t -test). This is representative of three SSc fibroblast strains examined in SUMO1 siRNA studies. * A , supercoiled DNA; B , relaxed DNA.

Article Snippet: Resolved proteins were transferred onto nitrocellulose membranes and incubated with 1:1,000 diluted primary antibodies including mouse anti-human topo I (ImmunoVision, Springdale, AR, USA), anti-human SUMO1 (ABGENT, San Diego, CA, USA) and anti-collagen type I, individually.

Techniques: Cell Culture, Transfection, Serial Dilution, Transformation Assay, Inhibition

Western blots show sumoylation of recombinant human topo I . Recombinant human topo I protein was subjected to the sumoylation reaction and examined by Western blotting using anti-topo I (I) and anti-SUMO1 antibodies (II). Compared to topo I protein without sumoylation reaction (topo I A ), topo I protein with sumoylation reaction (topo I B ) showed poly-sumoylation of topo I (II). The assays showed similar results in triplicates.

Journal: Arthritis Research & Therapy

Article Title: Decreased catalytic function with altered sumoylation of DNA topoisomerase I in the nuclei of scleroderma fibroblasts

doi: 10.1186/ar3435

Figure Lengend Snippet: Western blots show sumoylation of recombinant human topo I . Recombinant human topo I protein was subjected to the sumoylation reaction and examined by Western blotting using anti-topo I (I) and anti-SUMO1 antibodies (II). Compared to topo I protein without sumoylation reaction (topo I A ), topo I protein with sumoylation reaction (topo I B ) showed poly-sumoylation of topo I (II). The assays showed similar results in triplicates.

Article Snippet: Resolved proteins were transferred onto nitrocellulose membranes and incubated with 1:1,000 diluted primary antibodies including mouse anti-human topo I (ImmunoVision, Springdale, AR, USA), anti-human SUMO1 (ABGENT, San Diego, CA, USA) and anti-collagen type I, individually.

Techniques: Western Blot, Recombinant

Measurement of catalytic function of recombinant human topo I with and without sumoylation reaction . Recombinant human topo I proteins were sumoylated with either mutant sumo1 or wild type sumo1 or negative control (without sumoylation), and then were examined for their catalytic function in a serial dilution. Sumoylation of topo I with wild type sumo1 showed a reduction of efficiency in catalytic function (supercoiled DNA disappeared at the dilution of topo I concentration of 30) compared to the topo I protein sumoylated with mutant sumo1 or negative control (supercoiled DNA disappeared at topo I concentration of 22.5). This is representative of three assays. * A , standard supercoiled DNA band; B , standard relaxed DNA bands.

Journal: Arthritis Research & Therapy

Article Title: Decreased catalytic function with altered sumoylation of DNA topoisomerase I in the nuclei of scleroderma fibroblasts

doi: 10.1186/ar3435

Figure Lengend Snippet: Measurement of catalytic function of recombinant human topo I with and without sumoylation reaction . Recombinant human topo I proteins were sumoylated with either mutant sumo1 or wild type sumo1 or negative control (without sumoylation), and then were examined for their catalytic function in a serial dilution. Sumoylation of topo I with wild type sumo1 showed a reduction of efficiency in catalytic function (supercoiled DNA disappeared at the dilution of topo I concentration of 30) compared to the topo I protein sumoylated with mutant sumo1 or negative control (supercoiled DNA disappeared at topo I concentration of 22.5). This is representative of three assays. * A , standard supercoiled DNA band; B , standard relaxed DNA bands.

Article Snippet: Resolved proteins were transferred onto nitrocellulose membranes and incubated with 1:1,000 diluted primary antibodies including mouse anti-human topo I (ImmunoVision, Springdale, AR, USA), anti-human SUMO1 (ABGENT, San Diego, CA, USA) and anti-collagen type I, individually.

Techniques: Recombinant, Mutagenesis, Negative Control, Serial Dilution, Concentration Assay

Therapeutic benefit of Pml induction by IFNα or poly(I:C) through NEK1 t clearance in vivo . A) NEK1 t modification by SUMO1 and SUMO2/3. HEK293 cells were transfected with the indicated expression vectors and treated or not with IFNα. IP: immuno-precipitation, WCL: whole cell lysate. B) IFNα treatment induces proteasome-dependent degradation of NEK1 t in HEK293 cells. MG132: proteasome inhibitor, n=3. C) PML silencing impedes IFNα-induced NEK1 t degradation. Quantifications (right), n=3. D) Western blot of NEK1 t protein from the spinal cord of age-matched Nek1 t/t or Nek1 t/t Pml −/− mice following IFNα or poly(I:C) therapy, (*) non-specific band. E) IFNα or poly(I:C) therapy eliminates NEK1 t aggregates in αMNs of Nek1 t/t mice. Quantifications: ≥30 αMNs from ≥3 mice F) IFNα or poly(I:C) therapies selectively extend lifespan in Pml -proficient Nek1 t/t mice. Arrowhead: therapy initiation, continued until death. G) IFNα or poly(I:C) therapies improve muscle strength and neuromuscular function selectively in Pml -proficient Nek1 t/t ALS mice. Trendlines in Supplementary Fig.S2E.

Journal: bioRxiv

Article Title: ALS driven by mutant NEK1 aggregation is accelerated by Pml loss, but clinically reversed through pharmacologic induction of Pml -mediated degradation

doi: 10.1101/2024.11.23.622051

Figure Lengend Snippet: Therapeutic benefit of Pml induction by IFNα or poly(I:C) through NEK1 t clearance in vivo . A) NEK1 t modification by SUMO1 and SUMO2/3. HEK293 cells were transfected with the indicated expression vectors and treated or not with IFNα. IP: immuno-precipitation, WCL: whole cell lysate. B) IFNα treatment induces proteasome-dependent degradation of NEK1 t in HEK293 cells. MG132: proteasome inhibitor, n=3. C) PML silencing impedes IFNα-induced NEK1 t degradation. Quantifications (right), n=3. D) Western blot of NEK1 t protein from the spinal cord of age-matched Nek1 t/t or Nek1 t/t Pml −/− mice following IFNα or poly(I:C) therapy, (*) non-specific band. E) IFNα or poly(I:C) therapy eliminates NEK1 t aggregates in αMNs of Nek1 t/t mice. Quantifications: ≥30 αMNs from ≥3 mice F) IFNα or poly(I:C) therapies selectively extend lifespan in Pml -proficient Nek1 t/t mice. Arrowhead: therapy initiation, continued until death. G) IFNα or poly(I:C) therapies improve muscle strength and neuromuscular function selectively in Pml -proficient Nek1 t/t ALS mice. Trendlines in Supplementary Fig.S2E.

Article Snippet: The following antibodies were used for Western blots in HEK293 or Neuro2A cells: anti-GST (Cell signaling, Cat # 2624S), human anti-GAPDH (Santa Cruz, Cat # sc-32233;), human anti-actin (BioLegend, Cat # 622102), human anti-YY1 (Santa Cruz, H-10, Cat # sc-7341), human anti-PML (Santa Cruz, H-238, Cat # sc-5621 and Santa Cruz, E-11, Cat # sc-377390), human anti-SUMO1 (CST, Cat # 4930), human anti-SUMO2/3 (Abcam, Cat # ab3742).

Techniques: In Vivo, Modification, Transfection, Expressing, Immunoprecipitation, Western Blot