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senp5 protease domain  (Addgene inc)


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    Addgene inc senp5 protease domain
    ( A ) Size exclusion chromatography (SEC) curves exhibiting the formation of a complex between SENP3 protease domain 302 to 574aa and PELP1 SLiM -containing peptide 761 to 796aa. SDS-PAGE and total protein staining of SEC fractions are displayed below the x axis. ( B ) AlphaFold3 structural models of proSUMO substrates used in endopeptidase cleavage assays. Sequences of the proSUMO C-terminal tails (cleavage sites labeled with arrows) are shown below the structural models. ( C ) SDS-PAGE and total protein stain of in vitro SENP3 ± MBP-PELP1 SLiM endopeptidase activity assays against proSUMO1, −2, and −3 substrates. Decreasing concentrations (2500 to 0.12 nM) of SENP3 enzyme ± MBP-PELP1 761 to 796aa was incubated for 1 hour at 37°C with 5 μM proSUMO substrate. Cleaved proSUMO product is labeled with asterisks. Quantification curves representing percent (%) proSUMO endopeptidase cleavage correspond to the gel images and the enzyme concentration range was 1000 to 15.63 nM. SD was calculated from three independent experiments ( n = 3). ( D ) SDS-PAGE and total protein stain of in vitro SENP3 (C532A) ± MBP-PELP1 SLiM endopeptidase activity assay, illustrating no activity. ( E ) Quantification curves representing percent (%) proSUMO2 endopeptidase cleavage by SENP protease domain + PELP1 SLiM , SENP3 protease domain alone, or <t>SENP5</t> protease domain alone during a time course (0 to 450 s). Enzyme concentration was kept constant at 1000 nM along with substrate concentration at 5 μM. Percent cleavage was calculated as in (C). SD was calculated from three independent assay samples ( n = 3). Raw gel images are displayed in fig. S13A. ( F ) Differential scanning fluorimetry curves exhibiting the thermal stabilization of the SENP3 protease domain upon addition of short (“s,” amino acids 764 to 781) and long (“l,” amino acids 764 to 792) PELP1 SLIM peptides. Boltzmann and first derivative curves are shown on the top and bottom of the panel, respectively. Values for change in T m is only shown for the first derivative.
    Senp5 Protease Domain, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/senp5 protease domain/product/Addgene inc
    Average 93 stars, based on 5 article reviews
    senp5 protease domain - by Bioz Stars, 2026-06
    93/100 stars

    Images

    1) Product Images from "PELP1 coordinates the modular assembly and enzymatic activity of the rixosome complex"

    Article Title: PELP1 coordinates the modular assembly and enzymatic activity of the rixosome complex

    Journal: Science Advances

    doi: 10.1126/sciadv.adw4603

    ( A ) Size exclusion chromatography (SEC) curves exhibiting the formation of a complex between SENP3 protease domain 302 to 574aa and PELP1 SLiM -containing peptide 761 to 796aa. SDS-PAGE and total protein staining of SEC fractions are displayed below the x axis. ( B ) AlphaFold3 structural models of proSUMO substrates used in endopeptidase cleavage assays. Sequences of the proSUMO C-terminal tails (cleavage sites labeled with arrows) are shown below the structural models. ( C ) SDS-PAGE and total protein stain of in vitro SENP3 ± MBP-PELP1 SLiM endopeptidase activity assays against proSUMO1, −2, and −3 substrates. Decreasing concentrations (2500 to 0.12 nM) of SENP3 enzyme ± MBP-PELP1 761 to 796aa was incubated for 1 hour at 37°C with 5 μM proSUMO substrate. Cleaved proSUMO product is labeled with asterisks. Quantification curves representing percent (%) proSUMO endopeptidase cleavage correspond to the gel images and the enzyme concentration range was 1000 to 15.63 nM. SD was calculated from three independent experiments ( n = 3). ( D ) SDS-PAGE and total protein stain of in vitro SENP3 (C532A) ± MBP-PELP1 SLiM endopeptidase activity assay, illustrating no activity. ( E ) Quantification curves representing percent (%) proSUMO2 endopeptidase cleavage by SENP protease domain + PELP1 SLiM , SENP3 protease domain alone, or SENP5 protease domain alone during a time course (0 to 450 s). Enzyme concentration was kept constant at 1000 nM along with substrate concentration at 5 μM. Percent cleavage was calculated as in (C). SD was calculated from three independent assay samples ( n = 3). Raw gel images are displayed in fig. S13A. ( F ) Differential scanning fluorimetry curves exhibiting the thermal stabilization of the SENP3 protease domain upon addition of short (“s,” amino acids 764 to 781) and long (“l,” amino acids 764 to 792) PELP1 SLIM peptides. Boltzmann and first derivative curves are shown on the top and bottom of the panel, respectively. Values for change in T m is only shown for the first derivative.
    Figure Legend Snippet: ( A ) Size exclusion chromatography (SEC) curves exhibiting the formation of a complex between SENP3 protease domain 302 to 574aa and PELP1 SLiM -containing peptide 761 to 796aa. SDS-PAGE and total protein staining of SEC fractions are displayed below the x axis. ( B ) AlphaFold3 structural models of proSUMO substrates used in endopeptidase cleavage assays. Sequences of the proSUMO C-terminal tails (cleavage sites labeled with arrows) are shown below the structural models. ( C ) SDS-PAGE and total protein stain of in vitro SENP3 ± MBP-PELP1 SLiM endopeptidase activity assays against proSUMO1, −2, and −3 substrates. Decreasing concentrations (2500 to 0.12 nM) of SENP3 enzyme ± MBP-PELP1 761 to 796aa was incubated for 1 hour at 37°C with 5 μM proSUMO substrate. Cleaved proSUMO product is labeled with asterisks. Quantification curves representing percent (%) proSUMO endopeptidase cleavage correspond to the gel images and the enzyme concentration range was 1000 to 15.63 nM. SD was calculated from three independent experiments ( n = 3). ( D ) SDS-PAGE and total protein stain of in vitro SENP3 (C532A) ± MBP-PELP1 SLiM endopeptidase activity assay, illustrating no activity. ( E ) Quantification curves representing percent (%) proSUMO2 endopeptidase cleavage by SENP protease domain + PELP1 SLiM , SENP3 protease domain alone, or SENP5 protease domain alone during a time course (0 to 450 s). Enzyme concentration was kept constant at 1000 nM along with substrate concentration at 5 μM. Percent cleavage was calculated as in (C). SD was calculated from three independent assay samples ( n = 3). Raw gel images are displayed in fig. S13A. ( F ) Differential scanning fluorimetry curves exhibiting the thermal stabilization of the SENP3 protease domain upon addition of short (“s,” amino acids 764 to 781) and long (“l,” amino acids 764 to 792) PELP1 SLIM peptides. Boltzmann and first derivative curves are shown on the top and bottom of the panel, respectively. Values for change in T m is only shown for the first derivative.

    Techniques Used: Size-exclusion Chromatography, SDS Page, Staining, Labeling, In Vitro, Activity Assay, Incubation, Concentration Assay



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    senp5 protease domain  (Addgene inc)
    93
    Addgene inc senp5 protease domain
    ( A ) Size exclusion chromatography (SEC) curves exhibiting the formation of a complex between SENP3 protease domain 302 to 574aa and PELP1 SLiM -containing peptide 761 to 796aa. SDS-PAGE and total protein staining of SEC fractions are displayed below the x axis. ( B ) AlphaFold3 structural models of proSUMO substrates used in endopeptidase cleavage assays. Sequences of the proSUMO C-terminal tails (cleavage sites labeled with arrows) are shown below the structural models. ( C ) SDS-PAGE and total protein stain of in vitro SENP3 ± MBP-PELP1 SLiM endopeptidase activity assays against proSUMO1, −2, and −3 substrates. Decreasing concentrations (2500 to 0.12 nM) of SENP3 enzyme ± MBP-PELP1 761 to 796aa was incubated for 1 hour at 37°C with 5 μM proSUMO substrate. Cleaved proSUMO product is labeled with asterisks. Quantification curves representing percent (%) proSUMO endopeptidase cleavage correspond to the gel images and the enzyme concentration range was 1000 to 15.63 nM. SD was calculated from three independent experiments ( n = 3). ( D ) SDS-PAGE and total protein stain of in vitro SENP3 (C532A) ± MBP-PELP1 SLiM endopeptidase activity assay, illustrating no activity. ( E ) Quantification curves representing percent (%) proSUMO2 endopeptidase cleavage by SENP protease domain + PELP1 SLiM , SENP3 protease domain alone, or <t>SENP5</t> protease domain alone during a time course (0 to 450 s). Enzyme concentration was kept constant at 1000 nM along with substrate concentration at 5 μM. Percent cleavage was calculated as in (C). SD was calculated from three independent assay samples ( n = 3). Raw gel images are displayed in fig. S13A. ( F ) Differential scanning fluorimetry curves exhibiting the thermal stabilization of the SENP3 protease domain upon addition of short (“s,” amino acids 764 to 781) and long (“l,” amino acids 764 to 792) PELP1 SLIM peptides. Boltzmann and first derivative curves are shown on the top and bottom of the panel, respectively. Values for change in T m is only shown for the first derivative.
    Senp5 Protease Domain, supplied by Addgene 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/result/senp5 protease domain/product/Addgene inc
    Average 93 stars, based on 1 article reviews
    senp5 protease domain - by Bioz Stars, 2026-06
    93/100 stars
    		  Buy from Supplier

    Image Search Results


    ( A ) Size exclusion chromatography (SEC) curves exhibiting the formation of a complex between SENP3 protease domain 302 to 574aa and PELP1 SLiM -containing peptide 761 to 796aa. SDS-PAGE and total protein staining of SEC fractions are displayed below the x axis. ( B ) AlphaFold3 structural models of proSUMO substrates used in endopeptidase cleavage assays. Sequences of the proSUMO C-terminal tails (cleavage sites labeled with arrows) are shown below the structural models. ( C ) SDS-PAGE and total protein stain of in vitro SENP3 ± MBP-PELP1 SLiM endopeptidase activity assays against proSUMO1, −2, and −3 substrates. Decreasing concentrations (2500 to 0.12 nM) of SENP3 enzyme ± MBP-PELP1 761 to 796aa was incubated for 1 hour at 37°C with 5 μM proSUMO substrate. Cleaved proSUMO product is labeled with asterisks. Quantification curves representing percent (%) proSUMO endopeptidase cleavage correspond to the gel images and the enzyme concentration range was 1000 to 15.63 nM. SD was calculated from three independent experiments ( n = 3). ( D ) SDS-PAGE and total protein stain of in vitro SENP3 (C532A) ± MBP-PELP1 SLiM endopeptidase activity assay, illustrating no activity. ( E ) Quantification curves representing percent (%) proSUMO2 endopeptidase cleavage by SENP protease domain + PELP1 SLiM , SENP3 protease domain alone, or SENP5 protease domain alone during a time course (0 to 450 s). Enzyme concentration was kept constant at 1000 nM along with substrate concentration at 5 μM. Percent cleavage was calculated as in (C). SD was calculated from three independent assay samples ( n = 3). Raw gel images are displayed in fig. S13A. ( F ) Differential scanning fluorimetry curves exhibiting the thermal stabilization of the SENP3 protease domain upon addition of short (“s,” amino acids 764 to 781) and long (“l,” amino acids 764 to 792) PELP1 SLIM peptides. Boltzmann and first derivative curves are shown on the top and bottom of the panel, respectively. Values for change in T m is only shown for the first derivative.

    Journal: Science Advances

    Article Title: PELP1 coordinates the modular assembly and enzymatic activity of the rixosome complex

    doi: 10.1126/sciadv.adw4603

    Figure Lengend Snippet: ( A ) Size exclusion chromatography (SEC) curves exhibiting the formation of a complex between SENP3 protease domain 302 to 574aa and PELP1 SLiM -containing peptide 761 to 796aa. SDS-PAGE and total protein staining of SEC fractions are displayed below the x axis. ( B ) AlphaFold3 structural models of proSUMO substrates used in endopeptidase cleavage assays. Sequences of the proSUMO C-terminal tails (cleavage sites labeled with arrows) are shown below the structural models. ( C ) SDS-PAGE and total protein stain of in vitro SENP3 ± MBP-PELP1 SLiM endopeptidase activity assays against proSUMO1, −2, and −3 substrates. Decreasing concentrations (2500 to 0.12 nM) of SENP3 enzyme ± MBP-PELP1 761 to 796aa was incubated for 1 hour at 37°C with 5 μM proSUMO substrate. Cleaved proSUMO product is labeled with asterisks. Quantification curves representing percent (%) proSUMO endopeptidase cleavage correspond to the gel images and the enzyme concentration range was 1000 to 15.63 nM. SD was calculated from three independent experiments ( n = 3). ( D ) SDS-PAGE and total protein stain of in vitro SENP3 (C532A) ± MBP-PELP1 SLiM endopeptidase activity assay, illustrating no activity. ( E ) Quantification curves representing percent (%) proSUMO2 endopeptidase cleavage by SENP protease domain + PELP1 SLiM , SENP3 protease domain alone, or SENP5 protease domain alone during a time course (0 to 450 s). Enzyme concentration was kept constant at 1000 nM along with substrate concentration at 5 μM. Percent cleavage was calculated as in (C). SD was calculated from three independent assay samples ( n = 3). Raw gel images are displayed in fig. S13A. ( F ) Differential scanning fluorimetry curves exhibiting the thermal stabilization of the SENP3 protease domain upon addition of short (“s,” amino acids 764 to 781) and long (“l,” amino acids 764 to 792) PELP1 SLIM peptides. Boltzmann and first derivative curves are shown on the top and bottom of the panel, respectively. Values for change in T m is only shown for the first derivative.

    Article Snippet: N-terminal 6× His-tagged human SENP3 protease domain (302 to 574aa, E. coli codon-optimized gene synthesized by Genscript in pET11a vector) and SENP5 protease domain [567 to 755aa, plasmid no. 16358 ( ) from Addgene in pET28a vector] were used for in vitro binding and deSUMOylation assays.

    Techniques: Size-exclusion Chromatography, SDS Page, Staining, Labeling, In Vitro, Activity Assay, Incubation, Concentration Assay