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antibody recognizes phosphorylated ser 5 ctd  (GenScript corporation)

 
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    Structured Review

    GenScript corporation antibody recognizes phosphorylated ser 5 ctd
    ( A ) Structural organization of Med12. The first and second helices (orange ribbon) in Med12N are labeled as H1 and H2, respectively. Five HEAT domains (Med12HEAT) are shown in transparent surface. ( B ) Domain organization of Med12. The N- and C-terminal regions of Med12 (Med12N and Med12C) that form interactions with Cdk8/CycC and Med13, respectively, are indicated. Colors are as in (A). ( C ) Interactions of Med12 with Cdk8, CycC, and Med13. Cdk8, CycC, and Med13 are shown in colored surface representations. ( D ) The Med12 N-terminal region (residues 1 to 105) associates with Cdk8/CycC. GST-Med12 fragments in Escherichia coli lysates as indicated were immobilized on glutathione Sepharose beads and incubated with yeast cell lysate (CycC-TAP/Med12Δ/Med13Δ) containing Cdk8/CycC. ( E ) Kinase activity of yeast Cdk8/CycC stimulated by GST-Med12-(1–105). Phosphorylation of <t>GST-CTD-6xHis</t> was detected by the antibody that <t>recognizes</t> <t>phosphorylated</t> Ser 5 of CTD. For GST-Med12-(1–105), 250 ng (+) or 1 μg (++) of protein was used in the reactions. ( F ) Immunoprecipitation (IP) assay. Deletion of the C-terminal region (residues 1346 to 1427) of Med12 caused loss of Med13 from CKM.
    Antibody Recognizes Phosphorylated Ser 5 Ctd, supplied by GenScript corporation, 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/result/antibody recognizes phosphorylated ser 5 ctd/product/GenScript corporation
    Average 90 stars, based on 1 article reviews
    antibody recognizes phosphorylated ser 5 ctd - by Bioz Stars, 2026-04
    90/100 stars

    Images

    1) Product Images from "Structure and noncanonical Cdk8 activation mechanism within an Argonaute-containing Mediator kinase module"

    Article Title: Structure and noncanonical Cdk8 activation mechanism within an Argonaute-containing Mediator kinase module

    Journal: Science Advances

    doi: 10.1126/sciadv.abd4484

    ( A ) Structural organization of Med12. The first and second helices (orange ribbon) in Med12N are labeled as H1 and H2, respectively. Five HEAT domains (Med12HEAT) are shown in transparent surface. ( B ) Domain organization of Med12. The N- and C-terminal regions of Med12 (Med12N and Med12C) that form interactions with Cdk8/CycC and Med13, respectively, are indicated. Colors are as in (A). ( C ) Interactions of Med12 with Cdk8, CycC, and Med13. Cdk8, CycC, and Med13 are shown in colored surface representations. ( D ) The Med12 N-terminal region (residues 1 to 105) associates with Cdk8/CycC. GST-Med12 fragments in Escherichia coli lysates as indicated were immobilized on glutathione Sepharose beads and incubated with yeast cell lysate (CycC-TAP/Med12Δ/Med13Δ) containing Cdk8/CycC. ( E ) Kinase activity of yeast Cdk8/CycC stimulated by GST-Med12-(1–105). Phosphorylation of GST-CTD-6xHis was detected by the antibody that recognizes phosphorylated Ser 5 of CTD. For GST-Med12-(1–105), 250 ng (+) or 1 μg (++) of protein was used in the reactions. ( F ) Immunoprecipitation (IP) assay. Deletion of the C-terminal region (residues 1346 to 1427) of Med12 caused loss of Med13 from CKM.
    Figure Legend Snippet: ( A ) Structural organization of Med12. The first and second helices (orange ribbon) in Med12N are labeled as H1 and H2, respectively. Five HEAT domains (Med12HEAT) are shown in transparent surface. ( B ) Domain organization of Med12. The N- and C-terminal regions of Med12 (Med12N and Med12C) that form interactions with Cdk8/CycC and Med13, respectively, are indicated. Colors are as in (A). ( C ) Interactions of Med12 with Cdk8, CycC, and Med13. Cdk8, CycC, and Med13 are shown in colored surface representations. ( D ) The Med12 N-terminal region (residues 1 to 105) associates with Cdk8/CycC. GST-Med12 fragments in Escherichia coli lysates as indicated were immobilized on glutathione Sepharose beads and incubated with yeast cell lysate (CycC-TAP/Med12Δ/Med13Δ) containing Cdk8/CycC. ( E ) Kinase activity of yeast Cdk8/CycC stimulated by GST-Med12-(1–105). Phosphorylation of GST-CTD-6xHis was detected by the antibody that recognizes phosphorylated Ser 5 of CTD. For GST-Med12-(1–105), 250 ng (+) or 1 μg (++) of protein was used in the reactions. ( F ) Immunoprecipitation (IP) assay. Deletion of the C-terminal region (residues 1346 to 1427) of Med12 caused loss of Med13 from CKM.

    Techniques Used: Labeling, Incubation, Activity Assay, Phospho-proteomics, Immunoprecipitation



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    antibody recognizes phosphorylated ser 5 ctd  (GenScript corporation)
    90
    GenScript corporation antibody recognizes phosphorylated ser 5 ctd
    ( A ) Structural organization of Med12. The first and second helices (orange ribbon) in Med12N are labeled as H1 and H2, respectively. Five HEAT domains (Med12HEAT) are shown in transparent surface. ( B ) Domain organization of Med12. The N- and C-terminal regions of Med12 (Med12N and Med12C) that form interactions with Cdk8/CycC and Med13, respectively, are indicated. Colors are as in (A). ( C ) Interactions of Med12 with Cdk8, CycC, and Med13. Cdk8, CycC, and Med13 are shown in colored surface representations. ( D ) The Med12 N-terminal region (residues 1 to 105) associates with Cdk8/CycC. GST-Med12 fragments in Escherichia coli lysates as indicated were immobilized on glutathione Sepharose beads and incubated with yeast cell lysate (CycC-TAP/Med12Δ/Med13Δ) containing Cdk8/CycC. ( E ) Kinase activity of yeast Cdk8/CycC stimulated by GST-Med12-(1–105). Phosphorylation of <t>GST-CTD-6xHis</t> was detected by the antibody that <t>recognizes</t> <t>phosphorylated</t> Ser 5 of CTD. For GST-Med12-(1–105), 250 ng (+) or 1 μg (++) of protein was used in the reactions. ( F ) Immunoprecipitation (IP) assay. Deletion of the C-terminal region (residues 1346 to 1427) of Med12 caused loss of Med13 from CKM.
    Antibody Recognizes Phosphorylated Ser 5 Ctd, supplied by GenScript corporation, 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/result/antibody recognizes phosphorylated ser 5 ctd/product/GenScript corporation
    Average 90 stars, based on 1 article reviews
    antibody recognizes phosphorylated ser 5 ctd - by Bioz Stars, 2026-04
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    ( A ) Structural organization of Med12. The first and second helices (orange ribbon) in Med12N are labeled as H1 and H2, respectively. Five HEAT domains (Med12HEAT) are shown in transparent surface. ( B ) Domain organization of Med12. The N- and C-terminal regions of Med12 (Med12N and Med12C) that form interactions with Cdk8/CycC and Med13, respectively, are indicated. Colors are as in (A). ( C ) Interactions of Med12 with Cdk8, CycC, and Med13. Cdk8, CycC, and Med13 are shown in colored surface representations. ( D ) The Med12 N-terminal region (residues 1 to 105) associates with Cdk8/CycC. GST-Med12 fragments in Escherichia coli lysates as indicated were immobilized on glutathione Sepharose beads and incubated with yeast cell lysate (CycC-TAP/Med12Δ/Med13Δ) containing Cdk8/CycC. ( E ) Kinase activity of yeast Cdk8/CycC stimulated by GST-Med12-(1–105). Phosphorylation of GST-CTD-6xHis was detected by the antibody that recognizes phosphorylated Ser 5 of CTD. For GST-Med12-(1–105), 250 ng (+) or 1 μg (++) of protein was used in the reactions. ( F ) Immunoprecipitation (IP) assay. Deletion of the C-terminal region (residues 1346 to 1427) of Med12 caused loss of Med13 from CKM.

    Journal: Science Advances

    Article Title: Structure and noncanonical Cdk8 activation mechanism within an Argonaute-containing Mediator kinase module

    doi: 10.1126/sciadv.abd4484

    Figure Lengend Snippet: ( A ) Structural organization of Med12. The first and second helices (orange ribbon) in Med12N are labeled as H1 and H2, respectively. Five HEAT domains (Med12HEAT) are shown in transparent surface. ( B ) Domain organization of Med12. The N- and C-terminal regions of Med12 (Med12N and Med12C) that form interactions with Cdk8/CycC and Med13, respectively, are indicated. Colors are as in (A). ( C ) Interactions of Med12 with Cdk8, CycC, and Med13. Cdk8, CycC, and Med13 are shown in colored surface representations. ( D ) The Med12 N-terminal region (residues 1 to 105) associates with Cdk8/CycC. GST-Med12 fragments in Escherichia coli lysates as indicated were immobilized on glutathione Sepharose beads and incubated with yeast cell lysate (CycC-TAP/Med12Δ/Med13Δ) containing Cdk8/CycC. ( E ) Kinase activity of yeast Cdk8/CycC stimulated by GST-Med12-(1–105). Phosphorylation of GST-CTD-6xHis was detected by the antibody that recognizes phosphorylated Ser 5 of CTD. For GST-Med12-(1–105), 250 ng (+) or 1 μg (++) of protein was used in the reactions. ( F ) Immunoprecipitation (IP) assay. Deletion of the C-terminal region (residues 1346 to 1427) of Med12 caused loss of Med13 from CKM.

    Article Snippet: The antibody that recognizes phosphorylated Ser 5 of CTD (GenScript, A10634) was used to detect CTD phosphorylation.

    Techniques: Labeling, Incubation, Activity Assay, Phospho-proteomics, Immunoprecipitation