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sumo-conjugating enzyme sce  (Geiss)

 
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    Geiss sumo-conjugating enzyme sce
    A recombinant <t>SUMO</t> conjugation system generated with maize components. Various combinations of SUMO1a, the SAE1 and SAE2a polypeptides of the E1 heterodimer, and the SCE1b and SCE1f E2 enzymes bearing 6His, HA, FLAG, and Myc epitopes were expressed in E. coli. Crude extracts prepared after an 8-h induction at 30°C were probed with antibodies against AtSUMO1 (6His-SUMO1a), HA (HA-SAE1), FLAG (SAE2a-FLAG), and Myc (SCE1-Myc; right gel) or anti-6His antibodies (6His-SUMO1a; left gel). SCE1(C-S) indicates the Ser substitutions of the active-site Cys. A, The E1 and E2 enzymes are sufficient to drive SUMOylation. SUMO1a and the SAE1/2 heterodimer were coexpressed with wild-type or C-S versions of SCE1b (left gels) and an E. coli-optimized version of SCE1f (right gels). B, The truncated SAE2a splice variant T2 (Trunc) is functional but less active than full-length SAE2a (FL). The SAE2a polypeptides bearing a C-terminal FLAG tag were coexpressed individually with SUMO1a, SAE1, and SCE1b. Asterisk locates the T2 SAE2a truncation. C, Direct comparison of the <t>conjugating</t> activity of the class II E2 SCE1f with representative class I E2s, SCE1b, and SCE1d. D, Both class I and class II SCE1s catalyze the formation of poly-SUMO chains. Wild-type SUMO1a (WT) or the Lys-less K0 mutant blocked in forming SUMO chains were coexpressed with the SAE1/2 heterodimer and either SCE1b or SCE1f.
    Sumo Conjugating Enzyme Sce, supplied by Geiss, 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/sumo-conjugating+enzyme+sce/sumo+conjugating+enzyme+sce/pmc04936565-20-21-33
    Average 90 stars, based on 1 article reviews
    sumo-conjugating enzyme sce - by Bioz Stars, 2026-09
    90/100 stars

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    1) Product Images from "Defining the SUMO System in Maize: SUMOylation Is Up-Regulated during Endosperm Development and Rapidly Induced by Stress 1 [OPEN] "

    Article Title: Defining the SUMO System in Maize: SUMOylation Is Up-Regulated during Endosperm Development and Rapidly Induced by Stress 1 [OPEN]

    Journal: Plant Physiology

    doi: 10.1104/pp.16.00353

    A recombinant SUMO conjugation system generated with maize components. Various combinations of SUMO1a, the SAE1 and SAE2a polypeptides of the E1 heterodimer, and the SCE1b and SCE1f E2 enzymes bearing 6His, HA, FLAG, and Myc epitopes were expressed in E. coli. Crude extracts prepared after an 8-h induction at 30°C were probed with antibodies against AtSUMO1 (6His-SUMO1a), HA (HA-SAE1), FLAG (SAE2a-FLAG), and Myc (SCE1-Myc; right gel) or anti-6His antibodies (6His-SUMO1a; left gel). SCE1(C-S) indicates the Ser substitutions of the active-site Cys. A, The E1 and E2 enzymes are sufficient to drive SUMOylation. SUMO1a and the SAE1/2 heterodimer were coexpressed with wild-type or C-S versions of SCE1b (left gels) and an E. coli-optimized version of SCE1f (right gels). B, The truncated SAE2a splice variant T2 (Trunc) is functional but less active than full-length SAE2a (FL). The SAE2a polypeptides bearing a C-terminal FLAG tag were coexpressed individually with SUMO1a, SAE1, and SCE1b. Asterisk locates the T2 SAE2a truncation. C, Direct comparison of the conjugating activity of the class II E2 SCE1f with representative class I E2s, SCE1b, and SCE1d. D, Both class I and class II SCE1s catalyze the formation of poly-SUMO chains. Wild-type SUMO1a (WT) or the Lys-less K0 mutant blocked in forming SUMO chains were coexpressed with the SAE1/2 heterodimer and either SCE1b or SCE1f.
    Figure Legend Snippet: A recombinant SUMO conjugation system generated with maize components. Various combinations of SUMO1a, the SAE1 and SAE2a polypeptides of the E1 heterodimer, and the SCE1b and SCE1f E2 enzymes bearing 6His, HA, FLAG, and Myc epitopes were expressed in E. coli. Crude extracts prepared after an 8-h induction at 30°C were probed with antibodies against AtSUMO1 (6His-SUMO1a), HA (HA-SAE1), FLAG (SAE2a-FLAG), and Myc (SCE1-Myc; right gel) or anti-6His antibodies (6His-SUMO1a; left gel). SCE1(C-S) indicates the Ser substitutions of the active-site Cys. A, The E1 and E2 enzymes are sufficient to drive SUMOylation. SUMO1a and the SAE1/2 heterodimer were coexpressed with wild-type or C-S versions of SCE1b (left gels) and an E. coli-optimized version of SCE1f (right gels). B, The truncated SAE2a splice variant T2 (Trunc) is functional but less active than full-length SAE2a (FL). The SAE2a polypeptides bearing a C-terminal FLAG tag were coexpressed individually with SUMO1a, SAE1, and SCE1b. Asterisk locates the T2 SAE2a truncation. C, Direct comparison of the conjugating activity of the class II E2 SCE1f with representative class I E2s, SCE1b, and SCE1d. D, Both class I and class II SCE1s catalyze the formation of poly-SUMO chains. Wild-type SUMO1a (WT) or the Lys-less K0 mutant blocked in forming SUMO chains were coexpressed with the SAE1/2 heterodimer and either SCE1b or SCE1f.

    Techniques Used: Recombinant, Conjugation Assay, Generated, Variant Assay, Functional Assay, FLAG-tag, Comparison, Activity Assay, Mutagenesis

    Related Articles

    Conjugation Assay:

    Article Title: Defining the SUMO System in Maize: SUMOylation Is Up-Regulated during Endosperm Development and Rapidly Induced by Stress
    Article Snippet: Analogous to ubiquitylation, SUMOylation is driven by an ATP-dependent E1→E2→E3 conjugation cascade sequentially involving a heterodimeric SUMO-activating enzyme (SAE1/2), a single SUMO-conjugating enzyme (SCE), and a small collection of SUMO protein ligases ( Geiss-Friedlander and Melchior, 2007 ; Jentsch and Psakhye, 2013 ).

    Recombinant:

    Article Title: Defining the SUMO System in Maize: SUMOylation Is Up-Regulated during Endosperm Development and Rapidly Induced by Stress
    Article Snippet: Analogous to ubiquitylation, SUMOylation is driven by an ATP-dependent E1→E2→E3 conjugation cascade sequentially involving a heterodimeric SUMO-activating enzyme (SAE1/2), a single SUMO-conjugating enzyme (SCE), and a small collection of SUMO protein ligases ( Geiss-Friedlander and Melchior, 2007 ; Jentsch and Psakhye, 2013 ).

    Generated:

    Article Title: Defining the SUMO System in Maize: SUMOylation Is Up-Regulated during Endosperm Development and Rapidly Induced by Stress
    Article Snippet: Analogous to ubiquitylation, SUMOylation is driven by an ATP-dependent E1→E2→E3 conjugation cascade sequentially involving a heterodimeric SUMO-activating enzyme (SAE1/2), a single SUMO-conjugating enzyme (SCE), and a small collection of SUMO protein ligases ( Geiss-Friedlander and Melchior, 2007 ; Jentsch and Psakhye, 2013 ).

    Variant Assay:

    Article Title: Defining the SUMO System in Maize: SUMOylation Is Up-Regulated during Endosperm Development and Rapidly Induced by Stress
    Article Snippet: Analogous to ubiquitylation, SUMOylation is driven by an ATP-dependent E1→E2→E3 conjugation cascade sequentially involving a heterodimeric SUMO-activating enzyme (SAE1/2), a single SUMO-conjugating enzyme (SCE), and a small collection of SUMO protein ligases ( Geiss-Friedlander and Melchior, 2007 ; Jentsch and Psakhye, 2013 ).

    Functional Assay:

    Article Title: Defining the SUMO System in Maize: SUMOylation Is Up-Regulated during Endosperm Development and Rapidly Induced by Stress
    Article Snippet: Analogous to ubiquitylation, SUMOylation is driven by an ATP-dependent E1→E2→E3 conjugation cascade sequentially involving a heterodimeric SUMO-activating enzyme (SAE1/2), a single SUMO-conjugating enzyme (SCE), and a small collection of SUMO protein ligases ( Geiss-Friedlander and Melchior, 2007 ; Jentsch and Psakhye, 2013 ).

    FLAG-tag:

    Article Title: Defining the SUMO System in Maize: SUMOylation Is Up-Regulated during Endosperm Development and Rapidly Induced by Stress
    Article Snippet: Analogous to ubiquitylation, SUMOylation is driven by an ATP-dependent E1→E2→E3 conjugation cascade sequentially involving a heterodimeric SUMO-activating enzyme (SAE1/2), a single SUMO-conjugating enzyme (SCE), and a small collection of SUMO protein ligases ( Geiss-Friedlander and Melchior, 2007 ; Jentsch and Psakhye, 2013 ).

    Comparison:

    Article Title: Defining the SUMO System in Maize: SUMOylation Is Up-Regulated during Endosperm Development and Rapidly Induced by Stress
    Article Snippet: Analogous to ubiquitylation, SUMOylation is driven by an ATP-dependent E1→E2→E3 conjugation cascade sequentially involving a heterodimeric SUMO-activating enzyme (SAE1/2), a single SUMO-conjugating enzyme (SCE), and a small collection of SUMO protein ligases ( Geiss-Friedlander and Melchior, 2007 ; Jentsch and Psakhye, 2013 ).

    Activity Assay:

    Article Title: Defining the SUMO System in Maize: SUMOylation Is Up-Regulated during Endosperm Development and Rapidly Induced by Stress
    Article Snippet: Analogous to ubiquitylation, SUMOylation is driven by an ATP-dependent E1→E2→E3 conjugation cascade sequentially involving a heterodimeric SUMO-activating enzyme (SAE1/2), a single SUMO-conjugating enzyme (SCE), and a small collection of SUMO protein ligases ( Geiss-Friedlander and Melchior, 2007 ; Jentsch and Psakhye, 2013 ).

    Mutagenesis:

    Article Title: Defining the SUMO System in Maize: SUMOylation Is Up-Regulated during Endosperm Development and Rapidly Induced by Stress
    Article Snippet: Analogous to ubiquitylation, SUMOylation is driven by an ATP-dependent E1→E2→E3 conjugation cascade sequentially involving a heterodimeric SUMO-activating enzyme (SAE1/2), a single SUMO-conjugating enzyme (SCE), and a small collection of SUMO protein ligases ( Geiss-Friedlander and Melchior, 2007 ; Jentsch and Psakhye, 2013 ).



    Similar Products

    sumo-conjugating enzyme sce  (Geiss)
    90
    Geiss sumo-conjugating enzyme sce
    A recombinant <t>SUMO</t> conjugation system generated with maize components. Various combinations of SUMO1a, the SAE1 and SAE2a polypeptides of the E1 heterodimer, and the SCE1b and SCE1f E2 enzymes bearing 6His, HA, FLAG, and Myc epitopes were expressed in E. coli. Crude extracts prepared after an 8-h induction at 30°C were probed with antibodies against AtSUMO1 (6His-SUMO1a), HA (HA-SAE1), FLAG (SAE2a-FLAG), and Myc (SCE1-Myc; right gel) or anti-6His antibodies (6His-SUMO1a; left gel). SCE1(C-S) indicates the Ser substitutions of the active-site Cys. A, The E1 and E2 enzymes are sufficient to drive SUMOylation. SUMO1a and the SAE1/2 heterodimer were coexpressed with wild-type or C-S versions of SCE1b (left gels) and an E. coli-optimized version of SCE1f (right gels). B, The truncated SAE2a splice variant T2 (Trunc) is functional but less active than full-length SAE2a (FL). The SAE2a polypeptides bearing a C-terminal FLAG tag were coexpressed individually with SUMO1a, SAE1, and SCE1b. Asterisk locates the T2 SAE2a truncation. C, Direct comparison of the <t>conjugating</t> activity of the class II E2 SCE1f with representative class I E2s, SCE1b, and SCE1d. D, Both class I and class II SCE1s catalyze the formation of poly-SUMO chains. Wild-type SUMO1a (WT) or the Lys-less K0 mutant blocked in forming SUMO chains were coexpressed with the SAE1/2 heterodimer and either SCE1b or SCE1f.
    Sumo Conjugating Enzyme Sce, supplied by Geiss, 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/sumo-conjugating+enzyme+sce/sumo+conjugating+enzyme+sce/pmc04936565-20-21-33
    Average 90 stars, based on 1 article reviews
    sumo-conjugating enzyme sce - by Bioz Stars, 2026-09
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    A recombinant SUMO conjugation system generated with maize components. Various combinations of SUMO1a, the SAE1 and SAE2a polypeptides of the E1 heterodimer, and the SCE1b and SCE1f E2 enzymes bearing 6His, HA, FLAG, and Myc epitopes were expressed in E. coli. Crude extracts prepared after an 8-h induction at 30°C were probed with antibodies against AtSUMO1 (6His-SUMO1a), HA (HA-SAE1), FLAG (SAE2a-FLAG), and Myc (SCE1-Myc; right gel) or anti-6His antibodies (6His-SUMO1a; left gel). SCE1(C-S) indicates the Ser substitutions of the active-site Cys. A, The E1 and E2 enzymes are sufficient to drive SUMOylation. SUMO1a and the SAE1/2 heterodimer were coexpressed with wild-type or C-S versions of SCE1b (left gels) and an E. coli-optimized version of SCE1f (right gels). B, The truncated SAE2a splice variant T2 (Trunc) is functional but less active than full-length SAE2a (FL). The SAE2a polypeptides bearing a C-terminal FLAG tag were coexpressed individually with SUMO1a, SAE1, and SCE1b. Asterisk locates the T2 SAE2a truncation. C, Direct comparison of the conjugating activity of the class II E2 SCE1f with representative class I E2s, SCE1b, and SCE1d. D, Both class I and class II SCE1s catalyze the formation of poly-SUMO chains. Wild-type SUMO1a (WT) or the Lys-less K0 mutant blocked in forming SUMO chains were coexpressed with the SAE1/2 heterodimer and either SCE1b or SCE1f.

    Journal: Plant Physiology

    Article Title: Defining the SUMO System in Maize: SUMOylation Is Up-Regulated during Endosperm Development and Rapidly Induced by Stress 1 [OPEN]

    doi: 10.1104/pp.16.00353

    Figure Lengend Snippet: A recombinant SUMO conjugation system generated with maize components. Various combinations of SUMO1a, the SAE1 and SAE2a polypeptides of the E1 heterodimer, and the SCE1b and SCE1f E2 enzymes bearing 6His, HA, FLAG, and Myc epitopes were expressed in E. coli. Crude extracts prepared after an 8-h induction at 30°C were probed with antibodies against AtSUMO1 (6His-SUMO1a), HA (HA-SAE1), FLAG (SAE2a-FLAG), and Myc (SCE1-Myc; right gel) or anti-6His antibodies (6His-SUMO1a; left gel). SCE1(C-S) indicates the Ser substitutions of the active-site Cys. A, The E1 and E2 enzymes are sufficient to drive SUMOylation. SUMO1a and the SAE1/2 heterodimer were coexpressed with wild-type or C-S versions of SCE1b (left gels) and an E. coli-optimized version of SCE1f (right gels). B, The truncated SAE2a splice variant T2 (Trunc) is functional but less active than full-length SAE2a (FL). The SAE2a polypeptides bearing a C-terminal FLAG tag were coexpressed individually with SUMO1a, SAE1, and SCE1b. Asterisk locates the T2 SAE2a truncation. C, Direct comparison of the conjugating activity of the class II E2 SCE1f with representative class I E2s, SCE1b, and SCE1d. D, Both class I and class II SCE1s catalyze the formation of poly-SUMO chains. Wild-type SUMO1a (WT) or the Lys-less K0 mutant blocked in forming SUMO chains were coexpressed with the SAE1/2 heterodimer and either SCE1b or SCE1f.

    Article Snippet: Analogous to ubiquitylation, SUMOylation is driven by an ATP-dependent E1→E2→E3 conjugation cascade sequentially involving a heterodimeric SUMO-activating enzyme (SAE1/2), a single SUMO-conjugating enzyme (SCE), and a small collection of SUMO protein ligases ( Geiss-Friedlander and Melchior, 2007 ; Jentsch and Psakhye, 2013 ).

    Techniques: Recombinant, Conjugation Assay, Generated, Variant Assay, Functional Assay, FLAG-tag, Comparison, Activity Assay, Mutagenesis