rabbit anti bag6  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit anti bag6
    VAPB interaction with FAF1 and p97 is stimulated upon proteasome inhibition. (A) Proteasome inhibition enhances ubiquitin, p97 and FAF1 binding to Flag-VAPB, while ASNA1 binding remains largely unchanged. U2OS cells expressing Flag-VAPB from a tetracycline-inducible promoter were grown in the presence of 100 ng/ml tetracycline for 24 hr or left untreated as a control. Flag-VAPB was immunoprecipitated using anti-Flag beads. (B) Proteasome inhibition enhances ubiquitin, p97 and FAF1 binding to endogenous VAPB, while ASNA1 binding was only slightly increased. Endogenous VAPB was immunoprecipitated from U2OS cells using anti-VAPB antibodies cross-linked to Protein A-beads. Uncoupled beads were used as control. (C, D) The binding of ubiquitinated proteins to VAPB is largely mediated by FAF1. U2OS cells were treated with the indicated siRNA oligos. Flag-VAPB (C) or endogenous VAPB (D) were immunoprecipitated as described above. Depletion of FAF1 strongly reduces the binding of ubiquitinated proteins to Flag- or endogenous VAPB. (E) The K87D M89D double mutant (KM-DD) of VAPB is defective in p97, FAF1, ASNA1 and ubiquitin binding. Flag-VAPB full-length WT, KM-DD and truncated, C-terminal half (C-Ter) and N-terminal half (MSP), were immunoprecipitated from U2OS cells. The MSP domain of VAPB is sufficient to interact with p97, FAF1 and ASNA1. KM-DD as well as the truncation lacking the MSP domain (C-Ter) are defective in binding poly-ubiquitinated proteins and seem to interact preferentially with oligo-ubiquitinated proteins. (F) The binding of ubiquitinated proteins to VAPB is reduced in cells treated with ASNA1 siRNA. U2OS cells expressing Flag-VAPB from a tetracycline-inducible promoter were treated with the indicated siRNA oligos. Depletion of ASNA1 reduces ubiquitin and <t>BAG6</t> binding, but not FAF1 binding, to Flag-VAPB. C-Ter, C-terminal half; IP, immunoprecipitate; KM-DD, K87D M89D double mutant; Luc, luciferase.
    Rabbit Anti Bag6, 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/result/rabbit anti bag6/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit anti bag6 - by Bioz Stars, 2023-03
    94/100 stars

    Images

    1) Product Images from "VAPB/ALS8 interacts with FFAT-like proteins including the p97 cofactor FAF1 and the ASNA1 ATPase"

    Article Title: VAPB/ALS8 interacts with FFAT-like proteins including the p97 cofactor FAF1 and the ASNA1 ATPase

    Journal: BMC Biology

    doi: 10.1186/1741-7007-12-39

    VAPB interaction with FAF1 and p97 is stimulated upon proteasome inhibition. (A) Proteasome inhibition enhances ubiquitin, p97 and FAF1 binding to Flag-VAPB, while ASNA1 binding remains largely unchanged. U2OS cells expressing Flag-VAPB from a tetracycline-inducible promoter were grown in the presence of 100 ng/ml tetracycline for 24 hr or left untreated as a control. Flag-VAPB was immunoprecipitated using anti-Flag beads. (B) Proteasome inhibition enhances ubiquitin, p97 and FAF1 binding to endogenous VAPB, while ASNA1 binding was only slightly increased. Endogenous VAPB was immunoprecipitated from U2OS cells using anti-VAPB antibodies cross-linked to Protein A-beads. Uncoupled beads were used as control. (C, D) The binding of ubiquitinated proteins to VAPB is largely mediated by FAF1. U2OS cells were treated with the indicated siRNA oligos. Flag-VAPB (C) or endogenous VAPB (D) were immunoprecipitated as described above. Depletion of FAF1 strongly reduces the binding of ubiquitinated proteins to Flag- or endogenous VAPB. (E) The K87D M89D double mutant (KM-DD) of VAPB is defective in p97, FAF1, ASNA1 and ubiquitin binding. Flag-VAPB full-length WT, KM-DD and truncated, C-terminal half (C-Ter) and N-terminal half (MSP), were immunoprecipitated from U2OS cells. The MSP domain of VAPB is sufficient to interact with p97, FAF1 and ASNA1. KM-DD as well as the truncation lacking the MSP domain (C-Ter) are defective in binding poly-ubiquitinated proteins and seem to interact preferentially with oligo-ubiquitinated proteins. (F) The binding of ubiquitinated proteins to VAPB is reduced in cells treated with ASNA1 siRNA. U2OS cells expressing Flag-VAPB from a tetracycline-inducible promoter were treated with the indicated siRNA oligos. Depletion of ASNA1 reduces ubiquitin and BAG6 binding, but not FAF1 binding, to Flag-VAPB. C-Ter, C-terminal half; IP, immunoprecipitate; KM-DD, K87D M89D double mutant; Luc, luciferase.
    Figure Legend Snippet: VAPB interaction with FAF1 and p97 is stimulated upon proteasome inhibition. (A) Proteasome inhibition enhances ubiquitin, p97 and FAF1 binding to Flag-VAPB, while ASNA1 binding remains largely unchanged. U2OS cells expressing Flag-VAPB from a tetracycline-inducible promoter were grown in the presence of 100 ng/ml tetracycline for 24 hr or left untreated as a control. Flag-VAPB was immunoprecipitated using anti-Flag beads. (B) Proteasome inhibition enhances ubiquitin, p97 and FAF1 binding to endogenous VAPB, while ASNA1 binding was only slightly increased. Endogenous VAPB was immunoprecipitated from U2OS cells using anti-VAPB antibodies cross-linked to Protein A-beads. Uncoupled beads were used as control. (C, D) The binding of ubiquitinated proteins to VAPB is largely mediated by FAF1. U2OS cells were treated with the indicated siRNA oligos. Flag-VAPB (C) or endogenous VAPB (D) were immunoprecipitated as described above. Depletion of FAF1 strongly reduces the binding of ubiquitinated proteins to Flag- or endogenous VAPB. (E) The K87D M89D double mutant (KM-DD) of VAPB is defective in p97, FAF1, ASNA1 and ubiquitin binding. Flag-VAPB full-length WT, KM-DD and truncated, C-terminal half (C-Ter) and N-terminal half (MSP), were immunoprecipitated from U2OS cells. The MSP domain of VAPB is sufficient to interact with p97, FAF1 and ASNA1. KM-DD as well as the truncation lacking the MSP domain (C-Ter) are defective in binding poly-ubiquitinated proteins and seem to interact preferentially with oligo-ubiquitinated proteins. (F) The binding of ubiquitinated proteins to VAPB is reduced in cells treated with ASNA1 siRNA. U2OS cells expressing Flag-VAPB from a tetracycline-inducible promoter were treated with the indicated siRNA oligos. Depletion of ASNA1 reduces ubiquitin and BAG6 binding, but not FAF1 binding, to Flag-VAPB. C-Ter, C-terminal half; IP, immunoprecipitate; KM-DD, K87D M89D double mutant; Luc, luciferase.

    Techniques Used: Inhibition, Binding Assay, Expressing, Immunoprecipitation, Mutagenesis, Luciferase

    TRC subunits were identified by mass spectrometry in Flag-FAF1 immunoprecipitates
    Figure Legend Snippet: TRC subunits were identified by mass spectrometry in Flag-FAF1 immunoprecipitates

    Techniques Used: Mass Spectrometry

    TRC complex subunits slightly accumulate in endogenous VAPB immunoprecipitates upon proteasome inhibition
    Figure Legend Snippet: TRC complex subunits slightly accumulate in endogenous VAPB immunoprecipitates upon proteasome inhibition

    Techniques Used:

    ASNA1 interacts with VAPB via a FFAT-like motif similar to FAF1. (A) Alignment of the FFAT-like motifs in human ASNA1 and FAF1. (B) Alignment of the FFAT-like motif of ASNA1 across species showing that it is highly conserved. (C) A point mutation in the FFAT-like motif of ASNA1 (F15A) abolishes its interaction with VAPB. WT and mutant Flag-ASNA1 were immunoprecipitated from U2OS cells using anti-Flag beads. (D) Indirect immunofluorescence of VAPB and Flag-ASNA1 WT. U2OS cells were transfected with Flag-ASNA1 WT for 24 hr. Flag-ASNA1 WT (red) is co-localized with VAPB (green) in a peri-nuclear area (enlarged window) suggesting an ER pattern. Scale bar is 10 μm. (E) ASNA1 interaction with FAF1 is strongly stimulated upon proteasome inhibition with MG132 and depends on the UBA domain. WT Flag-FAF1 and the indicated mutants were immunoprecipitated from U2OS cells. (F) G46R and G46A point mutations in ASNA1 abolish its interaction with BAG6 and strongly reduce its interaction with FAF1 and ubiquitin, most noticeably after MG132 treatment, but do not affect the interaction with VAPB. WT and mutant Flag-ASNA1 were immunoprecipitated from SH-SY5Y cells. DAPI, 4',6-diamidino-2-phenylindole; IP, immunoprecipitate; WT, wild type.
    Figure Legend Snippet: ASNA1 interacts with VAPB via a FFAT-like motif similar to FAF1. (A) Alignment of the FFAT-like motifs in human ASNA1 and FAF1. (B) Alignment of the FFAT-like motif of ASNA1 across species showing that it is highly conserved. (C) A point mutation in the FFAT-like motif of ASNA1 (F15A) abolishes its interaction with VAPB. WT and mutant Flag-ASNA1 were immunoprecipitated from U2OS cells using anti-Flag beads. (D) Indirect immunofluorescence of VAPB and Flag-ASNA1 WT. U2OS cells were transfected with Flag-ASNA1 WT for 24 hr. Flag-ASNA1 WT (red) is co-localized with VAPB (green) in a peri-nuclear area (enlarged window) suggesting an ER pattern. Scale bar is 10 μm. (E) ASNA1 interaction with FAF1 is strongly stimulated upon proteasome inhibition with MG132 and depends on the UBA domain. WT Flag-FAF1 and the indicated mutants were immunoprecipitated from U2OS cells. (F) G46R and G46A point mutations in ASNA1 abolish its interaction with BAG6 and strongly reduce its interaction with FAF1 and ubiquitin, most noticeably after MG132 treatment, but do not affect the interaction with VAPB. WT and mutant Flag-ASNA1 were immunoprecipitated from SH-SY5Y cells. DAPI, 4',6-diamidino-2-phenylindole; IP, immunoprecipitate; WT, wild type.

    Techniques Used: Mutagenesis, Immunoprecipitation, Immunofluorescence, Transfection, Inhibition

    rabbit anti bag6  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
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    Structured Review

    Cell Signaling Technology Inc rabbit anti bag6
    VAPB interaction with FAF1 and p97 is stimulated upon proteasome inhibition. (A) Proteasome inhibition enhances ubiquitin, p97 and FAF1 binding to Flag-VAPB, while ASNA1 binding remains largely unchanged. U2OS cells expressing Flag-VAPB from a tetracycline-inducible promoter were grown in the presence of 100 ng/ml tetracycline for 24 hr or left untreated as a control. Flag-VAPB was immunoprecipitated using anti-Flag beads. (B) Proteasome inhibition enhances ubiquitin, p97 and FAF1 binding to endogenous VAPB, while ASNA1 binding was only slightly increased. Endogenous VAPB was immunoprecipitated from U2OS cells using anti-VAPB antibodies cross-linked to Protein A-beads. Uncoupled beads were used as control. (C, D) The binding of ubiquitinated proteins to VAPB is largely mediated by FAF1. U2OS cells were treated with the indicated siRNA oligos. Flag-VAPB (C) or endogenous VAPB (D) were immunoprecipitated as described above. Depletion of FAF1 strongly reduces the binding of ubiquitinated proteins to Flag- or endogenous VAPB. (E) The K87D M89D double mutant (KM-DD) of VAPB is defective in p97, FAF1, ASNA1 and ubiquitin binding. Flag-VAPB full-length WT, KM-DD and truncated, C-terminal half (C-Ter) and N-terminal half (MSP), were immunoprecipitated from U2OS cells. The MSP domain of VAPB is sufficient to interact with p97, FAF1 and ASNA1. KM-DD as well as the truncation lacking the MSP domain (C-Ter) are defective in binding poly-ubiquitinated proteins and seem to interact preferentially with oligo-ubiquitinated proteins. (F) The binding of ubiquitinated proteins to VAPB is reduced in cells treated with ASNA1 siRNA. U2OS cells expressing Flag-VAPB from a tetracycline-inducible promoter were treated with the indicated siRNA oligos. Depletion of ASNA1 reduces ubiquitin and <t>BAG6</t> binding, but not FAF1 binding, to Flag-VAPB. C-Ter, C-terminal half; IP, immunoprecipitate; KM-DD, K87D M89D double mutant; Luc, luciferase.
    Rabbit Anti Bag6, 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/result/rabbit anti bag6/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit anti bag6 - by Bioz Stars, 2023-03
    94/100 stars

    Images

    1) Product Images from "VAPB/ALS8 interacts with FFAT-like proteins including the p97 cofactor FAF1 and the ASNA1 ATPase"

    Article Title: VAPB/ALS8 interacts with FFAT-like proteins including the p97 cofactor FAF1 and the ASNA1 ATPase

    Journal: BMC Biology

    doi: 10.1186/1741-7007-12-39

    VAPB interaction with FAF1 and p97 is stimulated upon proteasome inhibition. (A) Proteasome inhibition enhances ubiquitin, p97 and FAF1 binding to Flag-VAPB, while ASNA1 binding remains largely unchanged. U2OS cells expressing Flag-VAPB from a tetracycline-inducible promoter were grown in the presence of 100 ng/ml tetracycline for 24 hr or left untreated as a control. Flag-VAPB was immunoprecipitated using anti-Flag beads. (B) Proteasome inhibition enhances ubiquitin, p97 and FAF1 binding to endogenous VAPB, while ASNA1 binding was only slightly increased. Endogenous VAPB was immunoprecipitated from U2OS cells using anti-VAPB antibodies cross-linked to Protein A-beads. Uncoupled beads were used as control. (C, D) The binding of ubiquitinated proteins to VAPB is largely mediated by FAF1. U2OS cells were treated with the indicated siRNA oligos. Flag-VAPB (C) or endogenous VAPB (D) were immunoprecipitated as described above. Depletion of FAF1 strongly reduces the binding of ubiquitinated proteins to Flag- or endogenous VAPB. (E) The K87D M89D double mutant (KM-DD) of VAPB is defective in p97, FAF1, ASNA1 and ubiquitin binding. Flag-VAPB full-length WT, KM-DD and truncated, C-terminal half (C-Ter) and N-terminal half (MSP), were immunoprecipitated from U2OS cells. The MSP domain of VAPB is sufficient to interact with p97, FAF1 and ASNA1. KM-DD as well as the truncation lacking the MSP domain (C-Ter) are defective in binding poly-ubiquitinated proteins and seem to interact preferentially with oligo-ubiquitinated proteins. (F) The binding of ubiquitinated proteins to VAPB is reduced in cells treated with ASNA1 siRNA. U2OS cells expressing Flag-VAPB from a tetracycline-inducible promoter were treated with the indicated siRNA oligos. Depletion of ASNA1 reduces ubiquitin and BAG6 binding, but not FAF1 binding, to Flag-VAPB. C-Ter, C-terminal half; IP, immunoprecipitate; KM-DD, K87D M89D double mutant; Luc, luciferase.
    Figure Legend Snippet: VAPB interaction with FAF1 and p97 is stimulated upon proteasome inhibition. (A) Proteasome inhibition enhances ubiquitin, p97 and FAF1 binding to Flag-VAPB, while ASNA1 binding remains largely unchanged. U2OS cells expressing Flag-VAPB from a tetracycline-inducible promoter were grown in the presence of 100 ng/ml tetracycline for 24 hr or left untreated as a control. Flag-VAPB was immunoprecipitated using anti-Flag beads. (B) Proteasome inhibition enhances ubiquitin, p97 and FAF1 binding to endogenous VAPB, while ASNA1 binding was only slightly increased. Endogenous VAPB was immunoprecipitated from U2OS cells using anti-VAPB antibodies cross-linked to Protein A-beads. Uncoupled beads were used as control. (C, D) The binding of ubiquitinated proteins to VAPB is largely mediated by FAF1. U2OS cells were treated with the indicated siRNA oligos. Flag-VAPB (C) or endogenous VAPB (D) were immunoprecipitated as described above. Depletion of FAF1 strongly reduces the binding of ubiquitinated proteins to Flag- or endogenous VAPB. (E) The K87D M89D double mutant (KM-DD) of VAPB is defective in p97, FAF1, ASNA1 and ubiquitin binding. Flag-VAPB full-length WT, KM-DD and truncated, C-terminal half (C-Ter) and N-terminal half (MSP), were immunoprecipitated from U2OS cells. The MSP domain of VAPB is sufficient to interact with p97, FAF1 and ASNA1. KM-DD as well as the truncation lacking the MSP domain (C-Ter) are defective in binding poly-ubiquitinated proteins and seem to interact preferentially with oligo-ubiquitinated proteins. (F) The binding of ubiquitinated proteins to VAPB is reduced in cells treated with ASNA1 siRNA. U2OS cells expressing Flag-VAPB from a tetracycline-inducible promoter were treated with the indicated siRNA oligos. Depletion of ASNA1 reduces ubiquitin and BAG6 binding, but not FAF1 binding, to Flag-VAPB. C-Ter, C-terminal half; IP, immunoprecipitate; KM-DD, K87D M89D double mutant; Luc, luciferase.

    Techniques Used: Inhibition, Binding Assay, Expressing, Immunoprecipitation, Mutagenesis, Luciferase

    TRC subunits were identified by mass spectrometry in Flag-FAF1 immunoprecipitates
    Figure Legend Snippet: TRC subunits were identified by mass spectrometry in Flag-FAF1 immunoprecipitates

    Techniques Used: Mass Spectrometry

    TRC complex subunits slightly accumulate in endogenous VAPB immunoprecipitates upon proteasome inhibition
    Figure Legend Snippet: TRC complex subunits slightly accumulate in endogenous VAPB immunoprecipitates upon proteasome inhibition

    Techniques Used:

    ASNA1 interacts with VAPB via a FFAT-like motif similar to FAF1. (A) Alignment of the FFAT-like motifs in human ASNA1 and FAF1. (B) Alignment of the FFAT-like motif of ASNA1 across species showing that it is highly conserved. (C) A point mutation in the FFAT-like motif of ASNA1 (F15A) abolishes its interaction with VAPB. WT and mutant Flag-ASNA1 were immunoprecipitated from U2OS cells using anti-Flag beads. (D) Indirect immunofluorescence of VAPB and Flag-ASNA1 WT. U2OS cells were transfected with Flag-ASNA1 WT for 24 hr. Flag-ASNA1 WT (red) is co-localized with VAPB (green) in a peri-nuclear area (enlarged window) suggesting an ER pattern. Scale bar is 10 μm. (E) ASNA1 interaction with FAF1 is strongly stimulated upon proteasome inhibition with MG132 and depends on the UBA domain. WT Flag-FAF1 and the indicated mutants were immunoprecipitated from U2OS cells. (F) G46R and G46A point mutations in ASNA1 abolish its interaction with BAG6 and strongly reduce its interaction with FAF1 and ubiquitin, most noticeably after MG132 treatment, but do not affect the interaction with VAPB. WT and mutant Flag-ASNA1 were immunoprecipitated from SH-SY5Y cells. DAPI, 4',6-diamidino-2-phenylindole; IP, immunoprecipitate; WT, wild type.
    Figure Legend Snippet: ASNA1 interacts with VAPB via a FFAT-like motif similar to FAF1. (A) Alignment of the FFAT-like motifs in human ASNA1 and FAF1. (B) Alignment of the FFAT-like motif of ASNA1 across species showing that it is highly conserved. (C) A point mutation in the FFAT-like motif of ASNA1 (F15A) abolishes its interaction with VAPB. WT and mutant Flag-ASNA1 were immunoprecipitated from U2OS cells using anti-Flag beads. (D) Indirect immunofluorescence of VAPB and Flag-ASNA1 WT. U2OS cells were transfected with Flag-ASNA1 WT for 24 hr. Flag-ASNA1 WT (red) is co-localized with VAPB (green) in a peri-nuclear area (enlarged window) suggesting an ER pattern. Scale bar is 10 μm. (E) ASNA1 interaction with FAF1 is strongly stimulated upon proteasome inhibition with MG132 and depends on the UBA domain. WT Flag-FAF1 and the indicated mutants were immunoprecipitated from U2OS cells. (F) G46R and G46A point mutations in ASNA1 abolish its interaction with BAG6 and strongly reduce its interaction with FAF1 and ubiquitin, most noticeably after MG132 treatment, but do not affect the interaction with VAPB. WT and mutant Flag-ASNA1 were immunoprecipitated from SH-SY5Y cells. DAPI, 4',6-diamidino-2-phenylindole; IP, immunoprecipitate; WT, wild type.

    Techniques Used: Mutagenesis, Immunoprecipitation, Immunofluorescence, Transfection, Inhibition

    bag6  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
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    Cell Signaling Technology Inc bag6
    PERM1 is a novel transcription coactivator that functionally interacts with PGC-1α, <t>BAG6,</t> and KANK2. (A) Immunoprecipitation assays show that PERM1 binds to the transcriptional regulators ERRα, PGC-1α, ANKRD1, BAG6, KANK2, and TIF1β. Adenovirus Flag-tagged Perm1 (PERM1-Flag) was transduced to cardiomyocytes, and PERM1-bound proteins were pulled down by anti-Flag antibody. Immunoblotting confirmed the interaction of PERM1 with ERRα, PGC-1α, ANKRD1, BAG6, KANK2, and TIF1β. In contrast, TRX1, which was also identified through MS-based screening as a potential binding partner in transcription regulation, did not bind to PERM1. (B) Luciferase reporter gene assays show that the PERM1-induced transcriptional activation of the ERRE requires PGC-1α, BAG6, and KANK2 ( n = 7-9/group). Cardiomyocytes were transduced with 3xERRE-luc, followed by transfecting with either scrambled-siRNA (scr), siPGC-1α, siANKRD1, siBAG6, siKANK2, or TIF1β. (C) In vitro Gal4 assay shows the recruitment of PERM1 to a gene promoter induces transcriptional activation ( n = 6/group). Gal4-fused Perm1 (Gal4- Perm1 ) was expressed with UAS-luc, a reporter gene driven by Gal4 binding sequence, in cardiomyocytes. In control (scrambled-siRNA, “scr”), the reporter activity was significantly increased by Gal4- Perm1 , indicating that PERM1 can act as a transcription coactivator. Silencing of PGC-1α, BAG6, KANK2 inhibited the transcription activation by PERM1. (D) qPCR shows downregulation of ERR target genes by silencing BAG6 and KANK2 (siBag6 and siKank2) in cultured cardiomyocytes ( n = 4/group). (E) siRNA-mediated knockdown of PGC-1α, ANKRD1, BAG6, KANK2, or TIF1β were verified by western blotting analyses. (F) Hypothetical model of transcriptional regulation by PERM1 on the ERRE. PERM1 is localized to and activates the ERRE in ERR target genes through interacting with ERRα and the other transcriptional regulators BAG6, KANK2, and PGC-1α (* p < 0.05).
    Bag6, 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
    https://www.bioz.com/result/bag6/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    bag6 - by Bioz Stars, 2023-03
    86/100 stars

    Images

    1) Product Images from "PERM1 regulates energy metabolism in the heart via ERRα/PGC−1α axis"

    Article Title: PERM1 regulates energy metabolism in the heart via ERRα/PGC−1α axis

    Journal: Frontiers in Cardiovascular Medicine

    doi: 10.3389/fcvm.2022.1033457

    PERM1 is a novel transcription coactivator that functionally interacts with PGC-1α, BAG6, and KANK2. (A) Immunoprecipitation assays show that PERM1 binds to the transcriptional regulators ERRα, PGC-1α, ANKRD1, BAG6, KANK2, and TIF1β. Adenovirus Flag-tagged Perm1 (PERM1-Flag) was transduced to cardiomyocytes, and PERM1-bound proteins were pulled down by anti-Flag antibody. Immunoblotting confirmed the interaction of PERM1 with ERRα, PGC-1α, ANKRD1, BAG6, KANK2, and TIF1β. In contrast, TRX1, which was also identified through MS-based screening as a potential binding partner in transcription regulation, did not bind to PERM1. (B) Luciferase reporter gene assays show that the PERM1-induced transcriptional activation of the ERRE requires PGC-1α, BAG6, and KANK2 ( n = 7-9/group). Cardiomyocytes were transduced with 3xERRE-luc, followed by transfecting with either scrambled-siRNA (scr), siPGC-1α, siANKRD1, siBAG6, siKANK2, or TIF1β. (C) In vitro Gal4 assay shows the recruitment of PERM1 to a gene promoter induces transcriptional activation ( n = 6/group). Gal4-fused Perm1 (Gal4- Perm1 ) was expressed with UAS-luc, a reporter gene driven by Gal4 binding sequence, in cardiomyocytes. In control (scrambled-siRNA, “scr”), the reporter activity was significantly increased by Gal4- Perm1 , indicating that PERM1 can act as a transcription coactivator. Silencing of PGC-1α, BAG6, KANK2 inhibited the transcription activation by PERM1. (D) qPCR shows downregulation of ERR target genes by silencing BAG6 and KANK2 (siBag6 and siKank2) in cultured cardiomyocytes ( n = 4/group). (E) siRNA-mediated knockdown of PGC-1α, ANKRD1, BAG6, KANK2, or TIF1β were verified by western blotting analyses. (F) Hypothetical model of transcriptional regulation by PERM1 on the ERRE. PERM1 is localized to and activates the ERRE in ERR target genes through interacting with ERRα and the other transcriptional regulators BAG6, KANK2, and PGC-1α (* p < 0.05).
    Figure Legend Snippet: PERM1 is a novel transcription coactivator that functionally interacts with PGC-1α, BAG6, and KANK2. (A) Immunoprecipitation assays show that PERM1 binds to the transcriptional regulators ERRα, PGC-1α, ANKRD1, BAG6, KANK2, and TIF1β. Adenovirus Flag-tagged Perm1 (PERM1-Flag) was transduced to cardiomyocytes, and PERM1-bound proteins were pulled down by anti-Flag antibody. Immunoblotting confirmed the interaction of PERM1 with ERRα, PGC-1α, ANKRD1, BAG6, KANK2, and TIF1β. In contrast, TRX1, which was also identified through MS-based screening as a potential binding partner in transcription regulation, did not bind to PERM1. (B) Luciferase reporter gene assays show that the PERM1-induced transcriptional activation of the ERRE requires PGC-1α, BAG6, and KANK2 ( n = 7-9/group). Cardiomyocytes were transduced with 3xERRE-luc, followed by transfecting with either scrambled-siRNA (scr), siPGC-1α, siANKRD1, siBAG6, siKANK2, or TIF1β. (C) In vitro Gal4 assay shows the recruitment of PERM1 to a gene promoter induces transcriptional activation ( n = 6/group). Gal4-fused Perm1 (Gal4- Perm1 ) was expressed with UAS-luc, a reporter gene driven by Gal4 binding sequence, in cardiomyocytes. In control (scrambled-siRNA, “scr”), the reporter activity was significantly increased by Gal4- Perm1 , indicating that PERM1 can act as a transcription coactivator. Silencing of PGC-1α, BAG6, KANK2 inhibited the transcription activation by PERM1. (D) qPCR shows downregulation of ERR target genes by silencing BAG6 and KANK2 (siBag6 and siKank2) in cultured cardiomyocytes ( n = 4/group). (E) siRNA-mediated knockdown of PGC-1α, ANKRD1, BAG6, KANK2, or TIF1β were verified by western blotting analyses. (F) Hypothetical model of transcriptional regulation by PERM1 on the ERRE. PERM1 is localized to and activates the ERRE in ERR target genes through interacting with ERRα and the other transcriptional regulators BAG6, KANK2, and PGC-1α (* p < 0.05).

    Techniques Used: Immunoprecipitation, Western Blot, Binding Assay, Luciferase, Activation Assay, Transduction, In Vitro, Sequencing, Activity Assay, Cell Culture

    bat3  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc bat3
    Bat3, 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
    https://www.bioz.com/result/bat3/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    bat3 - by Bioz Stars, 2023-03
    86/100 stars

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    bat3  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
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    Structured Review

    Cell Signaling Technology Inc bat3
    CEACAM1 expression increased on Huh7.5.1 cells infected with JFH‐1 and decreased after treatment. (A) Expression of ligands for NK cells, such as <t>BAT3,</t> ICAM‐1, ICAM‐2, nectin‐2, PVR, MICA/B, ULBP1, ULBP2/5/6, ULBP3, HLA‐A, B, C, HLA‐E, HLA‐G and CEACAM1, was analyzed on Huh7.5.1 cells and Huh7.5.1 cells infected with JFH‐1 (Huh7.5.1/JFH‐1 cells). The dotted line represents Huh7.5.1 cells, the solid line represents Huh7.5.1/JFH‐1 cells, and the shaded area represents the isotype control. (B) CEACAM1 expression on Huh7.5.1 cells and Huh7.5.1/JFH‐1 cells was analyzed by flow cytometry (left panel, means ± SD, n = 4). CEACAM1 levels in the supernatants of Huh7.5.1 cells and Huh7.5.1/JFH‐1 cells were analyzed by ELISA (middle panel, means ± SD, n = 4). In addition, levels of the CEACAM1 mRNA in Huh7.5.1 cells and Huh7.5.1/JFH‐1 cells were analyzed by qRT‐PCR (right panel, means ± SD, n = 4). (C,D) CEACAM1 levels at the cell surface and in supernatants of Huh7.5.1/JFH‐1 cells were measured by flow cytometry and ELISA, respectively, at the indicated times after infection (means ± SD, n = 4). (E) Immunofluorescence staining for NS5A (green) and 4’,6‐diamidino‐2‐phenylindole (DAPI; blue) was performed in Huh7.5.1/JFH‐1 (left panel) cells and Huh7.5.1/JFH‐1 cells treated with BILN (right panel). Levels of JFH‐1 mRNA in Huh7.5.1/JFH‐1 cells before and after treatment were evaluated by qRT‐PCR (means ± SD, n = 4). (F) Analysis of Huh7.5.1 cells, Huh7.5.1 cells + BILN, Huh7.5.1/JFH‐1 cells, and Huh7.5.1/JFH‐1 cells + BILN. CEACAM1 expression on these cells was analyzed by flow cytometry (means ± SD, n = 4). Levels of CEACAM1 mRNA in these cells were evaluated by qRT‐PCR (means ± SD, n = 4). * P < 0.05.
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    1) Product Images from "CEACAM1 Is Associated With the Suppression of Natural Killer Cell Function in Patients With Chronic Hepatitis C"

    Article Title: CEACAM1 Is Associated With the Suppression of Natural Killer Cell Function in Patients With Chronic Hepatitis C

    Journal: Hepatology Communications

    doi: 10.1002/hep4.1240

    CEACAM1 expression increased on Huh7.5.1 cells infected with JFH‐1 and decreased after treatment. (A) Expression of ligands for NK cells, such as BAT3, ICAM‐1, ICAM‐2, nectin‐2, PVR, MICA/B, ULBP1, ULBP2/5/6, ULBP3, HLA‐A, B, C, HLA‐E, HLA‐G and CEACAM1, was analyzed on Huh7.5.1 cells and Huh7.5.1 cells infected with JFH‐1 (Huh7.5.1/JFH‐1 cells). The dotted line represents Huh7.5.1 cells, the solid line represents Huh7.5.1/JFH‐1 cells, and the shaded area represents the isotype control. (B) CEACAM1 expression on Huh7.5.1 cells and Huh7.5.1/JFH‐1 cells was analyzed by flow cytometry (left panel, means ± SD, n = 4). CEACAM1 levels in the supernatants of Huh7.5.1 cells and Huh7.5.1/JFH‐1 cells were analyzed by ELISA (middle panel, means ± SD, n = 4). In addition, levels of the CEACAM1 mRNA in Huh7.5.1 cells and Huh7.5.1/JFH‐1 cells were analyzed by qRT‐PCR (right panel, means ± SD, n = 4). (C,D) CEACAM1 levels at the cell surface and in supernatants of Huh7.5.1/JFH‐1 cells were measured by flow cytometry and ELISA, respectively, at the indicated times after infection (means ± SD, n = 4). (E) Immunofluorescence staining for NS5A (green) and 4’,6‐diamidino‐2‐phenylindole (DAPI; blue) was performed in Huh7.5.1/JFH‐1 (left panel) cells and Huh7.5.1/JFH‐1 cells treated with BILN (right panel). Levels of JFH‐1 mRNA in Huh7.5.1/JFH‐1 cells before and after treatment were evaluated by qRT‐PCR (means ± SD, n = 4). (F) Analysis of Huh7.5.1 cells, Huh7.5.1 cells + BILN, Huh7.5.1/JFH‐1 cells, and Huh7.5.1/JFH‐1 cells + BILN. CEACAM1 expression on these cells was analyzed by flow cytometry (means ± SD, n = 4). Levels of CEACAM1 mRNA in these cells were evaluated by qRT‐PCR (means ± SD, n = 4). * P < 0.05.
    Figure Legend Snippet: CEACAM1 expression increased on Huh7.5.1 cells infected with JFH‐1 and decreased after treatment. (A) Expression of ligands for NK cells, such as BAT3, ICAM‐1, ICAM‐2, nectin‐2, PVR, MICA/B, ULBP1, ULBP2/5/6, ULBP3, HLA‐A, B, C, HLA‐E, HLA‐G and CEACAM1, was analyzed on Huh7.5.1 cells and Huh7.5.1 cells infected with JFH‐1 (Huh7.5.1/JFH‐1 cells). The dotted line represents Huh7.5.1 cells, the solid line represents Huh7.5.1/JFH‐1 cells, and the shaded area represents the isotype control. (B) CEACAM1 expression on Huh7.5.1 cells and Huh7.5.1/JFH‐1 cells was analyzed by flow cytometry (left panel, means ± SD, n = 4). CEACAM1 levels in the supernatants of Huh7.5.1 cells and Huh7.5.1/JFH‐1 cells were analyzed by ELISA (middle panel, means ± SD, n = 4). In addition, levels of the CEACAM1 mRNA in Huh7.5.1 cells and Huh7.5.1/JFH‐1 cells were analyzed by qRT‐PCR (right panel, means ± SD, n = 4). (C,D) CEACAM1 levels at the cell surface and in supernatants of Huh7.5.1/JFH‐1 cells were measured by flow cytometry and ELISA, respectively, at the indicated times after infection (means ± SD, n = 4). (E) Immunofluorescence staining for NS5A (green) and 4’,6‐diamidino‐2‐phenylindole (DAPI; blue) was performed in Huh7.5.1/JFH‐1 (left panel) cells and Huh7.5.1/JFH‐1 cells treated with BILN (right panel). Levels of JFH‐1 mRNA in Huh7.5.1/JFH‐1 cells before and after treatment were evaluated by qRT‐PCR (means ± SD, n = 4). (F) Analysis of Huh7.5.1 cells, Huh7.5.1 cells + BILN, Huh7.5.1/JFH‐1 cells, and Huh7.5.1/JFH‐1 cells + BILN. CEACAM1 expression on these cells was analyzed by flow cytometry (means ± SD, n = 4). Levels of CEACAM1 mRNA in these cells were evaluated by qRT‐PCR (means ± SD, n = 4). * P < 0.05.

    Techniques Used: Expressing, Infection, Flow Cytometry, Enzyme-linked Immunosorbent Assay, Quantitative RT-PCR, Immunofluorescence, Staining

    bag6  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc bag6
    (A) 293T cells were transfected with FLAG-tagged UBQLN1 (MIG-PLIC1) and an empty vector control (EV) followed by immunoprecipitation and analysis by mass spectrometry. The data from one representative experiment is shown. The number of unique peptides identified for each UBQLN1-interacting protein is shown. (B) 293T cells were transfected with FLAG-tagged deletion constructs of UBQLN1 followed by immunoprecipitation by FLAG antibody and Western Blot analysis. Like BCLbWT, STI domains of UBQLN1 are required to interact with IGF1R and ESYT2 as UBQLN1112X missing the STI and UBA domains do not interact with these 2 substrates. UBQLN1WT, UBQLN1112X and UBQLN1ΔUBA interact with both PSMD4 and <t>BAG6</t> indicating that this interaction is UBL mediated. (C) Stability of IGF1R, ESYT2, PSMD4 and BAG6 were tested upon CH and MG132 exposure for 48 hours as with BCLb in Fig. 4. In the absence of the UBA domain (UBQLN1ΔUBA), IGF1R and ESYT2 expression are lost upon proteasomal inhibition with MG132. PSMD4 and BAG6 expression are unchanged after 48 hours of CH and MG132 and the presence of UBQLN1WT, UBQLN1112X or UBQLN1ΔUBA does not affect their stability.
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    1) Product Images from "The STI and UBA domains of UBQLN1 are critical determinants of substrate interaction and proteostasis"

    Article Title: The STI and UBA domains of UBQLN1 are critical determinants of substrate interaction and proteostasis

    Journal: Journal of cellular biochemistry

    doi: 10.1002/jcb.25880

    (A) 293T cells were transfected with FLAG-tagged UBQLN1 (MIG-PLIC1) and an empty vector control (EV) followed by immunoprecipitation and analysis by mass spectrometry. The data from one representative experiment is shown. The number of unique peptides identified for each UBQLN1-interacting protein is shown. (B) 293T cells were transfected with FLAG-tagged deletion constructs of UBQLN1 followed by immunoprecipitation by FLAG antibody and Western Blot analysis. Like BCLbWT, STI domains of UBQLN1 are required to interact with IGF1R and ESYT2 as UBQLN1112X missing the STI and UBA domains do not interact with these 2 substrates. UBQLN1WT, UBQLN1112X and UBQLN1ΔUBA interact with both PSMD4 and BAG6 indicating that this interaction is UBL mediated. (C) Stability of IGF1R, ESYT2, PSMD4 and BAG6 were tested upon CH and MG132 exposure for 48 hours as with BCLb in Fig. 4. In the absence of the UBA domain (UBQLN1ΔUBA), IGF1R and ESYT2 expression are lost upon proteasomal inhibition with MG132. PSMD4 and BAG6 expression are unchanged after 48 hours of CH and MG132 and the presence of UBQLN1WT, UBQLN1112X or UBQLN1ΔUBA does not affect their stability.
    Figure Legend Snippet: (A) 293T cells were transfected with FLAG-tagged UBQLN1 (MIG-PLIC1) and an empty vector control (EV) followed by immunoprecipitation and analysis by mass spectrometry. The data from one representative experiment is shown. The number of unique peptides identified for each UBQLN1-interacting protein is shown. (B) 293T cells were transfected with FLAG-tagged deletion constructs of UBQLN1 followed by immunoprecipitation by FLAG antibody and Western Blot analysis. Like BCLbWT, STI domains of UBQLN1 are required to interact with IGF1R and ESYT2 as UBQLN1112X missing the STI and UBA domains do not interact with these 2 substrates. UBQLN1WT, UBQLN1112X and UBQLN1ΔUBA interact with both PSMD4 and BAG6 indicating that this interaction is UBL mediated. (C) Stability of IGF1R, ESYT2, PSMD4 and BAG6 were tested upon CH and MG132 exposure for 48 hours as with BCLb in Fig. 4. In the absence of the UBA domain (UBQLN1ΔUBA), IGF1R and ESYT2 expression are lost upon proteasomal inhibition with MG132. PSMD4 and BAG6 expression are unchanged after 48 hours of CH and MG132 and the presence of UBQLN1WT, UBQLN1112X or UBQLN1ΔUBA does not affect their stability.

    Techniques Used: Transfection, Plasmid Preparation, Immunoprecipitation, Mass Spectrometry, Construct, Western Blot, Expressing, Inhibition

    bag6  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc bag6
    (A) 293T cells were transfected with FLAG-tagged UBQLN1 (MIG-PLIC1) and an empty vector control (EV) followed by immunoprecipitation and analysis by mass spectrometry. The data from one representative experiment is shown. The number of unique peptides identified for each UBQLN1-interacting protein is shown. (B) 293T cells were transfected with FLAG-tagged deletion constructs of UBQLN1 followed by immunoprecipitation by FLAG antibody and Western Blot analysis. Like BCLbWT, STI domains of UBQLN1 are required to interact with IGF1R and ESYT2 as UBQLN1112X missing the STI and UBA domains do not interact with these 2 substrates. UBQLN1WT, UBQLN1112X and UBQLN1ΔUBA interact with both PSMD4 and <t>BAG6</t> indicating that this interaction is UBL mediated. (C) Stability of IGF1R, ESYT2, PSMD4 and BAG6 were tested upon CH and MG132 exposure for 48 hours as with BCLb in Fig. 4. In the absence of the UBA domain (UBQLN1ΔUBA), IGF1R and ESYT2 expression are lost upon proteasomal inhibition with MG132. PSMD4 and BAG6 expression are unchanged after 48 hours of CH and MG132 and the presence of UBQLN1WT, UBQLN1112X or UBQLN1ΔUBA does not affect their stability.
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    1) Product Images from "The STI and UBA domains of UBQLN1 are critical determinants of substrate interaction and proteostasis"

    Article Title: The STI and UBA domains of UBQLN1 are critical determinants of substrate interaction and proteostasis

    Journal: Journal of cellular biochemistry

    doi: 10.1002/jcb.25880

    (A) 293T cells were transfected with FLAG-tagged UBQLN1 (MIG-PLIC1) and an empty vector control (EV) followed by immunoprecipitation and analysis by mass spectrometry. The data from one representative experiment is shown. The number of unique peptides identified for each UBQLN1-interacting protein is shown. (B) 293T cells were transfected with FLAG-tagged deletion constructs of UBQLN1 followed by immunoprecipitation by FLAG antibody and Western Blot analysis. Like BCLbWT, STI domains of UBQLN1 are required to interact with IGF1R and ESYT2 as UBQLN1112X missing the STI and UBA domains do not interact with these 2 substrates. UBQLN1WT, UBQLN1112X and UBQLN1ΔUBA interact with both PSMD4 and BAG6 indicating that this interaction is UBL mediated. (C) Stability of IGF1R, ESYT2, PSMD4 and BAG6 were tested upon CH and MG132 exposure for 48 hours as with BCLb in Fig. 4. In the absence of the UBA domain (UBQLN1ΔUBA), IGF1R and ESYT2 expression are lost upon proteasomal inhibition with MG132. PSMD4 and BAG6 expression are unchanged after 48 hours of CH and MG132 and the presence of UBQLN1WT, UBQLN1112X or UBQLN1ΔUBA does not affect their stability.
    Figure Legend Snippet: (A) 293T cells were transfected with FLAG-tagged UBQLN1 (MIG-PLIC1) and an empty vector control (EV) followed by immunoprecipitation and analysis by mass spectrometry. The data from one representative experiment is shown. The number of unique peptides identified for each UBQLN1-interacting protein is shown. (B) 293T cells were transfected with FLAG-tagged deletion constructs of UBQLN1 followed by immunoprecipitation by FLAG antibody and Western Blot analysis. Like BCLbWT, STI domains of UBQLN1 are required to interact with IGF1R and ESYT2 as UBQLN1112X missing the STI and UBA domains do not interact with these 2 substrates. UBQLN1WT, UBQLN1112X and UBQLN1ΔUBA interact with both PSMD4 and BAG6 indicating that this interaction is UBL mediated. (C) Stability of IGF1R, ESYT2, PSMD4 and BAG6 were tested upon CH and MG132 exposure for 48 hours as with BCLb in Fig. 4. In the absence of the UBA domain (UBQLN1ΔUBA), IGF1R and ESYT2 expression are lost upon proteasomal inhibition with MG132. PSMD4 and BAG6 expression are unchanged after 48 hours of CH and MG132 and the presence of UBQLN1WT, UBQLN1112X or UBQLN1ΔUBA does not affect their stability.

    Techniques Used: Transfection, Plasmid Preparation, Immunoprecipitation, Mass Spectrometry, Construct, Western Blot, Expressing, Inhibition

    bat3  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc bat3
    Tim-3 and Lag-3 pathways. a The Tim-3 pathway. Tim-3 is composed of an extracellular IgV domain, a mucin stalk with N- and O-linked glycosylation sites, and an intracellular tail with conserved tyrosine residues. It is expressed on T cells, NK cells, and APCs and binds to cell surface receptors (Ceacam-1 and phosphatidyl serine (PtdSer)) and soluble ligands (galectin-9 and HMGB1). Ligand binding triggers phosphorylation of two conserved tyrosine residues and release of <t>Bat3</t> from the cytoplasmic tail of Tim-3, allowing Tim-3 to exert its inhibitory function. b The Lag-3 pathway. Lag-3 is composed of four extracellular Ig-like domains, a transmembrane domain, and a cytoplasmic tail containing a unique KIEELE motif. It is expressed on T cells and NK cells and binds to MHC class II on APCs, galectin-3, and LSECtin on tumor cells or liver cells
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    1) Product Images from "Tim-3, Lag-3, and TIGIT"

    Article Title: Tim-3, Lag-3, and TIGIT

    Journal: Current topics in microbiology and immunology

    doi: 10.1007/82_2017_62

    Tim-3 and Lag-3 pathways. a The Tim-3 pathway. Tim-3 is composed of an extracellular IgV domain, a mucin stalk with N- and O-linked glycosylation sites, and an intracellular tail with conserved tyrosine residues. It is expressed on T cells, NK cells, and APCs and binds to cell surface receptors (Ceacam-1 and phosphatidyl serine (PtdSer)) and soluble ligands (galectin-9 and HMGB1). Ligand binding triggers phosphorylation of two conserved tyrosine residues and release of Bat3 from the cytoplasmic tail of Tim-3, allowing Tim-3 to exert its inhibitory function. b The Lag-3 pathway. Lag-3 is composed of four extracellular Ig-like domains, a transmembrane domain, and a cytoplasmic tail containing a unique KIEELE motif. It is expressed on T cells and NK cells and binds to MHC class II on APCs, galectin-3, and LSECtin on tumor cells or liver cells
    Figure Legend Snippet: Tim-3 and Lag-3 pathways. a The Tim-3 pathway. Tim-3 is composed of an extracellular IgV domain, a mucin stalk with N- and O-linked glycosylation sites, and an intracellular tail with conserved tyrosine residues. It is expressed on T cells, NK cells, and APCs and binds to cell surface receptors (Ceacam-1 and phosphatidyl serine (PtdSer)) and soluble ligands (galectin-9 and HMGB1). Ligand binding triggers phosphorylation of two conserved tyrosine residues and release of Bat3 from the cytoplasmic tail of Tim-3, allowing Tim-3 to exert its inhibitory function. b The Lag-3 pathway. Lag-3 is composed of four extracellular Ig-like domains, a transmembrane domain, and a cytoplasmic tail containing a unique KIEELE motif. It is expressed on T cells and NK cells and binds to MHC class II on APCs, galectin-3, and LSECtin on tumor cells or liver cells

    Techniques Used: Ligand Binding Assay

    bat3  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc bat3
    Tim-3 and Lag-3 pathways. a The Tim-3 pathway. Tim-3 is composed of an extracellular IgV domain, a mucin stalk with N- and O-linked glycosylation sites, and an intracellular tail with conserved tyrosine residues. It is expressed on T cells, NK cells, and APCs and binds to cell surface receptors (Ceacam-1 and phosphatidyl serine (PtdSer)) and soluble ligands (galectin-9 and HMGB1). Ligand binding triggers phosphorylation of two conserved tyrosine residues and release of <t>Bat3</t> from the cytoplasmic tail of Tim-3, allowing Tim-3 to exert its inhibitory function. b The Lag-3 pathway. Lag-3 is composed of four extracellular Ig-like domains, a transmembrane domain, and a cytoplasmic tail containing a unique KIEELE motif. It is expressed on T cells and NK cells and binds to MHC class II on APCs, galectin-3, and LSECtin on tumor cells or liver cells
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    1) Product Images from "Tim-3, Lag-3, and TIGIT"

    Article Title: Tim-3, Lag-3, and TIGIT

    Journal: Current topics in microbiology and immunology

    doi: 10.1007/82_2017_62

    Tim-3 and Lag-3 pathways. a The Tim-3 pathway. Tim-3 is composed of an extracellular IgV domain, a mucin stalk with N- and O-linked glycosylation sites, and an intracellular tail with conserved tyrosine residues. It is expressed on T cells, NK cells, and APCs and binds to cell surface receptors (Ceacam-1 and phosphatidyl serine (PtdSer)) and soluble ligands (galectin-9 and HMGB1). Ligand binding triggers phosphorylation of two conserved tyrosine residues and release of Bat3 from the cytoplasmic tail of Tim-3, allowing Tim-3 to exert its inhibitory function. b The Lag-3 pathway. Lag-3 is composed of four extracellular Ig-like domains, a transmembrane domain, and a cytoplasmic tail containing a unique KIEELE motif. It is expressed on T cells and NK cells and binds to MHC class II on APCs, galectin-3, and LSECtin on tumor cells or liver cells
    Figure Legend Snippet: Tim-3 and Lag-3 pathways. a The Tim-3 pathway. Tim-3 is composed of an extracellular IgV domain, a mucin stalk with N- and O-linked glycosylation sites, and an intracellular tail with conserved tyrosine residues. It is expressed on T cells, NK cells, and APCs and binds to cell surface receptors (Ceacam-1 and phosphatidyl serine (PtdSer)) and soluble ligands (galectin-9 and HMGB1). Ligand binding triggers phosphorylation of two conserved tyrosine residues and release of Bat3 from the cytoplasmic tail of Tim-3, allowing Tim-3 to exert its inhibitory function. b The Lag-3 pathway. Lag-3 is composed of four extracellular Ig-like domains, a transmembrane domain, and a cytoplasmic tail containing a unique KIEELE motif. It is expressed on T cells and NK cells and binds to MHC class II on APCs, galectin-3, and LSECtin on tumor cells or liver cells

    Techniques Used: Ligand Binding Assay

    bag6  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc bag6
    Bag6, 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
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    anti bag6  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti bag6
    The RBULs link posttranscriptional processes to the ubiquitin system. ( a ) The BP and MF GO terms of the interactors of the six RBULs were grouped into the categories “RNA” (blue), “Ubiquitin” (turquoise), and “Other” (rose). The distribution of the categories among the interactomes is shown. ( b ) A summary of GO terms for MEX3B interaction partners is shown. ( c , d ) Validation of RBUL interaction partners by pulldowns and Western blot. ( c ) Endogenous PRPF19 was pulled down with a PRPF19-specific antibody from HEK293T cells. Experiments omitting the antibody served as control. Western blot analysis was performed with antibodies specific against BAG2, <t>BAG6,</t> VCP, and HSPA1A, as well as against PRPF19 itself to validate the immunoprecipitation (IP). Left: Cropped images of input and IP samples (replicate 1). Images of full membranes and different exposure times for all antibodies and replicates are presented in Supplementary Figure . Right: Quantifications of the PRPF19-specific IPs normalized to control of three independent biological replicates are shown in a dot plot, including mean and standard error (s.e.m.). ( d ) GFP (empty vector, EV) and GFP-MEX3B were expressed in HEK293T cells and pulled down with a GFP-specific antibody. Western blot analysis was performed using specific antibodies against POLR1A, POLR3A, VCP, and HSPA1A, as well as GFP. Left: Cropped images of input and AP samples (replicate 1). Images of full membranes and different exposure times for all antibodies are presented in Supplementary Figure . Right: Quantification of the APs normalized to EV are shown as in ( c ).
    Anti Bag6, 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
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    1) Product Images from "Interaction profiling of RNA-binding ubiquitin ligases reveals a link between posttranscriptional regulation and the ubiquitin system"

    Article Title: Interaction profiling of RNA-binding ubiquitin ligases reveals a link between posttranscriptional regulation and the ubiquitin system

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-16695-6

    The RBULs link posttranscriptional processes to the ubiquitin system. ( a ) The BP and MF GO terms of the interactors of the six RBULs were grouped into the categories “RNA” (blue), “Ubiquitin” (turquoise), and “Other” (rose). The distribution of the categories among the interactomes is shown. ( b ) A summary of GO terms for MEX3B interaction partners is shown. ( c , d ) Validation of RBUL interaction partners by pulldowns and Western blot. ( c ) Endogenous PRPF19 was pulled down with a PRPF19-specific antibody from HEK293T cells. Experiments omitting the antibody served as control. Western blot analysis was performed with antibodies specific against BAG2, BAG6, VCP, and HSPA1A, as well as against PRPF19 itself to validate the immunoprecipitation (IP). Left: Cropped images of input and IP samples (replicate 1). Images of full membranes and different exposure times for all antibodies and replicates are presented in Supplementary Figure . Right: Quantifications of the PRPF19-specific IPs normalized to control of three independent biological replicates are shown in a dot plot, including mean and standard error (s.e.m.). ( d ) GFP (empty vector, EV) and GFP-MEX3B were expressed in HEK293T cells and pulled down with a GFP-specific antibody. Western blot analysis was performed using specific antibodies against POLR1A, POLR3A, VCP, and HSPA1A, as well as GFP. Left: Cropped images of input and AP samples (replicate 1). Images of full membranes and different exposure times for all antibodies are presented in Supplementary Figure . Right: Quantification of the APs normalized to EV are shown as in ( c ).
    Figure Legend Snippet: The RBULs link posttranscriptional processes to the ubiquitin system. ( a ) The BP and MF GO terms of the interactors of the six RBULs were grouped into the categories “RNA” (blue), “Ubiquitin” (turquoise), and “Other” (rose). The distribution of the categories among the interactomes is shown. ( b ) A summary of GO terms for MEX3B interaction partners is shown. ( c , d ) Validation of RBUL interaction partners by pulldowns and Western blot. ( c ) Endogenous PRPF19 was pulled down with a PRPF19-specific antibody from HEK293T cells. Experiments omitting the antibody served as control. Western blot analysis was performed with antibodies specific against BAG2, BAG6, VCP, and HSPA1A, as well as against PRPF19 itself to validate the immunoprecipitation (IP). Left: Cropped images of input and IP samples (replicate 1). Images of full membranes and different exposure times for all antibodies and replicates are presented in Supplementary Figure . Right: Quantifications of the PRPF19-specific IPs normalized to control of three independent biological replicates are shown in a dot plot, including mean and standard error (s.e.m.). ( d ) GFP (empty vector, EV) and GFP-MEX3B were expressed in HEK293T cells and pulled down with a GFP-specific antibody. Western blot analysis was performed using specific antibodies against POLR1A, POLR3A, VCP, and HSPA1A, as well as GFP. Left: Cropped images of input and AP samples (replicate 1). Images of full membranes and different exposure times for all antibodies are presented in Supplementary Figure . Right: Quantification of the APs normalized to EV are shown as in ( c ).

    Techniques Used: Western Blot, Immunoprecipitation, Plasmid Preparation

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    • rabbit anti bag6  (Cell Signaling Technology Inc)
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    VAPB interaction with FAF1 and p97 is stimulated upon proteasome inhibition. (A) Proteasome inhibition enhances ubiquitin, p97 and FAF1 binding to Flag-VAPB, while ASNA1 binding remains largely unchanged. U2OS cells expressing Flag-VAPB from a tetracycline-inducible promoter were grown in the presence of 100 ng/ml tetracycline for 24 hr or left untreated as a control. Flag-VAPB was immunoprecipitated using anti-Flag beads. (B) Proteasome inhibition enhances ubiquitin, p97 and FAF1 binding to endogenous VAPB, while ASNA1 binding was only slightly increased. Endogenous VAPB was immunoprecipitated from U2OS cells using anti-VAPB antibodies cross-linked to Protein A-beads. Uncoupled beads were used as control. (C, D) The binding of ubiquitinated proteins to VAPB is largely mediated by FAF1. U2OS cells were treated with the indicated siRNA oligos. Flag-VAPB (C) or endogenous VAPB (D) were immunoprecipitated as described above. Depletion of FAF1 strongly reduces the binding of ubiquitinated proteins to Flag- or endogenous VAPB. (E) The K87D M89D double mutant (KM-DD) of VAPB is defective in p97, FAF1, ASNA1 and ubiquitin binding. Flag-VAPB full-length WT, KM-DD and truncated, C-terminal half (C-Ter) and N-terminal half (MSP), were immunoprecipitated from U2OS cells. The MSP domain of VAPB is sufficient to interact with p97, FAF1 and ASNA1. KM-DD as well as the truncation lacking the MSP domain (C-Ter) are defective in binding poly-ubiquitinated proteins and seem to interact preferentially with oligo-ubiquitinated proteins. (F) The binding of ubiquitinated proteins to VAPB is reduced in cells treated with ASNA1 siRNA. U2OS cells expressing Flag-VAPB from a tetracycline-inducible promoter were treated with the indicated siRNA oligos. Depletion of ASNA1 reduces ubiquitin and <t>BAG6</t> binding, but not FAF1 binding, to Flag-VAPB. C-Ter, C-terminal half; IP, immunoprecipitate; KM-DD, K87D M89D double mutant; Luc, luciferase.
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    bag6  (Cell Signaling Technology Inc)
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    PERM1 is a novel transcription coactivator that functionally interacts with PGC-1α, <t>BAG6,</t> and KANK2. (A) Immunoprecipitation assays show that PERM1 binds to the transcriptional regulators ERRα, PGC-1α, ANKRD1, BAG6, KANK2, and TIF1β. Adenovirus Flag-tagged Perm1 (PERM1-Flag) was transduced to cardiomyocytes, and PERM1-bound proteins were pulled down by anti-Flag antibody. Immunoblotting confirmed the interaction of PERM1 with ERRα, PGC-1α, ANKRD1, BAG6, KANK2, and TIF1β. In contrast, TRX1, which was also identified through MS-based screening as a potential binding partner in transcription regulation, did not bind to PERM1. (B) Luciferase reporter gene assays show that the PERM1-induced transcriptional activation of the ERRE requires PGC-1α, BAG6, and KANK2 ( n = 7-9/group). Cardiomyocytes were transduced with 3xERRE-luc, followed by transfecting with either scrambled-siRNA (scr), siPGC-1α, siANKRD1, siBAG6, siKANK2, or TIF1β. (C) In vitro Gal4 assay shows the recruitment of PERM1 to a gene promoter induces transcriptional activation ( n = 6/group). Gal4-fused Perm1 (Gal4- Perm1 ) was expressed with UAS-luc, a reporter gene driven by Gal4 binding sequence, in cardiomyocytes. In control (scrambled-siRNA, “scr”), the reporter activity was significantly increased by Gal4- Perm1 , indicating that PERM1 can act as a transcription coactivator. Silencing of PGC-1α, BAG6, KANK2 inhibited the transcription activation by PERM1. (D) qPCR shows downregulation of ERR target genes by silencing BAG6 and KANK2 (siBag6 and siKank2) in cultured cardiomyocytes ( n = 4/group). (E) siRNA-mediated knockdown of PGC-1α, ANKRD1, BAG6, KANK2, or TIF1β were verified by western blotting analyses. (F) Hypothetical model of transcriptional regulation by PERM1 on the ERRE. PERM1 is localized to and activates the ERRE in ERR target genes through interacting with ERRα and the other transcriptional regulators BAG6, KANK2, and PGC-1α (* p < 0.05).
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    bat3  (Cell Signaling Technology Inc)
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    PERM1 is a novel transcription coactivator that functionally interacts with PGC-1α, <t>BAG6,</t> and KANK2. (A) Immunoprecipitation assays show that PERM1 binds to the transcriptional regulators ERRα, PGC-1α, ANKRD1, BAG6, KANK2, and TIF1β. Adenovirus Flag-tagged Perm1 (PERM1-Flag) was transduced to cardiomyocytes, and PERM1-bound proteins were pulled down by anti-Flag antibody. Immunoblotting confirmed the interaction of PERM1 with ERRα, PGC-1α, ANKRD1, BAG6, KANK2, and TIF1β. In contrast, TRX1, which was also identified through MS-based screening as a potential binding partner in transcription regulation, did not bind to PERM1. (B) Luciferase reporter gene assays show that the PERM1-induced transcriptional activation of the ERRE requires PGC-1α, BAG6, and KANK2 ( n = 7-9/group). Cardiomyocytes were transduced with 3xERRE-luc, followed by transfecting with either scrambled-siRNA (scr), siPGC-1α, siANKRD1, siBAG6, siKANK2, or TIF1β. (C) In vitro Gal4 assay shows the recruitment of PERM1 to a gene promoter induces transcriptional activation ( n = 6/group). Gal4-fused Perm1 (Gal4- Perm1 ) was expressed with UAS-luc, a reporter gene driven by Gal4 binding sequence, in cardiomyocytes. In control (scrambled-siRNA, “scr”), the reporter activity was significantly increased by Gal4- Perm1 , indicating that PERM1 can act as a transcription coactivator. Silencing of PGC-1α, BAG6, KANK2 inhibited the transcription activation by PERM1. (D) qPCR shows downregulation of ERR target genes by silencing BAG6 and KANK2 (siBag6 and siKank2) in cultured cardiomyocytes ( n = 4/group). (E) siRNA-mediated knockdown of PGC-1α, ANKRD1, BAG6, KANK2, or TIF1β were verified by western blotting analyses. (F) Hypothetical model of transcriptional regulation by PERM1 on the ERRE. PERM1 is localized to and activates the ERRE in ERR target genes through interacting with ERRα and the other transcriptional regulators BAG6, KANK2, and PGC-1α (* p < 0.05).
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    anti bag6  (Cell Signaling Technology Inc)
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    The RBULs link posttranscriptional processes to the ubiquitin system. ( a ) The BP and MF GO terms of the interactors of the six RBULs were grouped into the categories “RNA” (blue), “Ubiquitin” (turquoise), and “Other” (rose). The distribution of the categories among the interactomes is shown. ( b ) A summary of GO terms for MEX3B interaction partners is shown. ( c , d ) Validation of RBUL interaction partners by pulldowns and Western blot. ( c ) Endogenous PRPF19 was pulled down with a PRPF19-specific antibody from HEK293T cells. Experiments omitting the antibody served as control. Western blot analysis was performed with antibodies specific against BAG2, <t>BAG6,</t> VCP, and HSPA1A, as well as against PRPF19 itself to validate the immunoprecipitation (IP). Left: Cropped images of input and IP samples (replicate 1). Images of full membranes and different exposure times for all antibodies and replicates are presented in Supplementary Figure . Right: Quantifications of the PRPF19-specific IPs normalized to control of three independent biological replicates are shown in a dot plot, including mean and standard error (s.e.m.). ( d ) GFP (empty vector, EV) and GFP-MEX3B were expressed in HEK293T cells and pulled down with a GFP-specific antibody. Western blot analysis was performed using specific antibodies against POLR1A, POLR3A, VCP, and HSPA1A, as well as GFP. Left: Cropped images of input and AP samples (replicate 1). Images of full membranes and different exposure times for all antibodies are presented in Supplementary Figure . Right: Quantification of the APs normalized to EV are shown as in ( c ).
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    VAPB interaction with FAF1 and p97 is stimulated upon proteasome inhibition. (A) Proteasome inhibition enhances ubiquitin, p97 and FAF1 binding to Flag-VAPB, while ASNA1 binding remains largely unchanged. U2OS cells expressing Flag-VAPB from a tetracycline-inducible promoter were grown in the presence of 100 ng/ml tetracycline for 24 hr or left untreated as a control. Flag-VAPB was immunoprecipitated using anti-Flag beads. (B) Proteasome inhibition enhances ubiquitin, p97 and FAF1 binding to endogenous VAPB, while ASNA1 binding was only slightly increased. Endogenous VAPB was immunoprecipitated from U2OS cells using anti-VAPB antibodies cross-linked to Protein A-beads. Uncoupled beads were used as control. (C, D) The binding of ubiquitinated proteins to VAPB is largely mediated by FAF1. U2OS cells were treated with the indicated siRNA oligos. Flag-VAPB (C) or endogenous VAPB (D) were immunoprecipitated as described above. Depletion of FAF1 strongly reduces the binding of ubiquitinated proteins to Flag- or endogenous VAPB. (E) The K87D M89D double mutant (KM-DD) of VAPB is defective in p97, FAF1, ASNA1 and ubiquitin binding. Flag-VAPB full-length WT, KM-DD and truncated, C-terminal half (C-Ter) and N-terminal half (MSP), were immunoprecipitated from U2OS cells. The MSP domain of VAPB is sufficient to interact with p97, FAF1 and ASNA1. KM-DD as well as the truncation lacking the MSP domain (C-Ter) are defective in binding poly-ubiquitinated proteins and seem to interact preferentially with oligo-ubiquitinated proteins. (F) The binding of ubiquitinated proteins to VAPB is reduced in cells treated with ASNA1 siRNA. U2OS cells expressing Flag-VAPB from a tetracycline-inducible promoter were treated with the indicated siRNA oligos. Depletion of ASNA1 reduces ubiquitin and BAG6 binding, but not FAF1 binding, to Flag-VAPB. C-Ter, C-terminal half; IP, immunoprecipitate; KM-DD, K87D M89D double mutant; Luc, luciferase.

    Journal: BMC Biology

    Article Title: VAPB/ALS8 interacts with FFAT-like proteins including the p97 cofactor FAF1 and the ASNA1 ATPase

    doi: 10.1186/1741-7007-12-39

    Figure Lengend Snippet: VAPB interaction with FAF1 and p97 is stimulated upon proteasome inhibition. (A) Proteasome inhibition enhances ubiquitin, p97 and FAF1 binding to Flag-VAPB, while ASNA1 binding remains largely unchanged. U2OS cells expressing Flag-VAPB from a tetracycline-inducible promoter were grown in the presence of 100 ng/ml tetracycline for 24 hr or left untreated as a control. Flag-VAPB was immunoprecipitated using anti-Flag beads. (B) Proteasome inhibition enhances ubiquitin, p97 and FAF1 binding to endogenous VAPB, while ASNA1 binding was only slightly increased. Endogenous VAPB was immunoprecipitated from U2OS cells using anti-VAPB antibodies cross-linked to Protein A-beads. Uncoupled beads were used as control. (C, D) The binding of ubiquitinated proteins to VAPB is largely mediated by FAF1. U2OS cells were treated with the indicated siRNA oligos. Flag-VAPB (C) or endogenous VAPB (D) were immunoprecipitated as described above. Depletion of FAF1 strongly reduces the binding of ubiquitinated proteins to Flag- or endogenous VAPB. (E) The K87D M89D double mutant (KM-DD) of VAPB is defective in p97, FAF1, ASNA1 and ubiquitin binding. Flag-VAPB full-length WT, KM-DD and truncated, C-terminal half (C-Ter) and N-terminal half (MSP), were immunoprecipitated from U2OS cells. The MSP domain of VAPB is sufficient to interact with p97, FAF1 and ASNA1. KM-DD as well as the truncation lacking the MSP domain (C-Ter) are defective in binding poly-ubiquitinated proteins and seem to interact preferentially with oligo-ubiquitinated proteins. (F) The binding of ubiquitinated proteins to VAPB is reduced in cells treated with ASNA1 siRNA. U2OS cells expressing Flag-VAPB from a tetracycline-inducible promoter were treated with the indicated siRNA oligos. Depletion of ASNA1 reduces ubiquitin and BAG6 binding, but not FAF1 binding, to Flag-VAPB. C-Ter, C-terminal half; IP, immunoprecipitate; KM-DD, K87D M89D double mutant; Luc, luciferase.

    Article Snippet: The following antibodies were used: mouse anti-Flag M2 (Sigma, A8592), mouse anti-ubiquitin FK2 (Enzo, PW8810), rabbit anti-ubiquitin (Dako, Ely, UK; Z0458), mouse anti-p97 (Fitzgerald, North Acton, USA; 10R-P104A), rabbit anti-VAPA (Epitomics, Burlingame, USA; S1706), mouse anti-FAF1 (Abnova, Taipei City, Taiwan; H00011124-A01), rabbit anti-FAF1 (courtesy of Millipore, Billerica, USA), rabbit anti-GAPDH (Cell Signaling, 2118), rabbit anti-RAB3GAP1 (Proteintech, Manchester, UK; 21663-1-AP), rabbit anti-RAB3GAP2 (Abgent, Maidenhead, UK; AP9635B), rabbit anti-WDR44 (Bethyl, Montgomery, USA; A301-441A), mouse anti-ASNA1 (Abnova, H00000439-M03), rabbit anti-Syntaxin 1A (GeneTex, Irvine, USA; GTX113559), rabbit anti-BAG6 (Cell Signaling, 8523S), mouse anti-RPN2 (Abnova, H00006185-B01), rabbit anti-CD147 (Abcam, Cambridge, UK; ab108317), Alexa Fluor® 488 goat anti-rabbit (Invitrogen, A11008) and Alexa Fluor® 594 chicken anti-mouse (Invitrogen, A21201).

    Techniques: Inhibition, Binding Assay, Expressing, Immunoprecipitation, Mutagenesis, Luciferase

    TRC subunits were identified by mass spectrometry in Flag-FAF1 immunoprecipitates

    Journal: BMC Biology

    Article Title: VAPB/ALS8 interacts with FFAT-like proteins including the p97 cofactor FAF1 and the ASNA1 ATPase

    doi: 10.1186/1741-7007-12-39

    Figure Lengend Snippet: TRC subunits were identified by mass spectrometry in Flag-FAF1 immunoprecipitates

    Article Snippet: The following antibodies were used: mouse anti-Flag M2 (Sigma, A8592), mouse anti-ubiquitin FK2 (Enzo, PW8810), rabbit anti-ubiquitin (Dako, Ely, UK; Z0458), mouse anti-p97 (Fitzgerald, North Acton, USA; 10R-P104A), rabbit anti-VAPA (Epitomics, Burlingame, USA; S1706), mouse anti-FAF1 (Abnova, Taipei City, Taiwan; H00011124-A01), rabbit anti-FAF1 (courtesy of Millipore, Billerica, USA), rabbit anti-GAPDH (Cell Signaling, 2118), rabbit anti-RAB3GAP1 (Proteintech, Manchester, UK; 21663-1-AP), rabbit anti-RAB3GAP2 (Abgent, Maidenhead, UK; AP9635B), rabbit anti-WDR44 (Bethyl, Montgomery, USA; A301-441A), mouse anti-ASNA1 (Abnova, H00000439-M03), rabbit anti-Syntaxin 1A (GeneTex, Irvine, USA; GTX113559), rabbit anti-BAG6 (Cell Signaling, 8523S), mouse anti-RPN2 (Abnova, H00006185-B01), rabbit anti-CD147 (Abcam, Cambridge, UK; ab108317), Alexa Fluor® 488 goat anti-rabbit (Invitrogen, A11008) and Alexa Fluor® 594 chicken anti-mouse (Invitrogen, A21201).

    Techniques: Mass Spectrometry

    TRC complex subunits slightly accumulate in endogenous VAPB immunoprecipitates upon proteasome inhibition

    Journal: BMC Biology

    Article Title: VAPB/ALS8 interacts with FFAT-like proteins including the p97 cofactor FAF1 and the ASNA1 ATPase

    doi: 10.1186/1741-7007-12-39

    Figure Lengend Snippet: TRC complex subunits slightly accumulate in endogenous VAPB immunoprecipitates upon proteasome inhibition

    Article Snippet: The following antibodies were used: mouse anti-Flag M2 (Sigma, A8592), mouse anti-ubiquitin FK2 (Enzo, PW8810), rabbit anti-ubiquitin (Dako, Ely, UK; Z0458), mouse anti-p97 (Fitzgerald, North Acton, USA; 10R-P104A), rabbit anti-VAPA (Epitomics, Burlingame, USA; S1706), mouse anti-FAF1 (Abnova, Taipei City, Taiwan; H00011124-A01), rabbit anti-FAF1 (courtesy of Millipore, Billerica, USA), rabbit anti-GAPDH (Cell Signaling, 2118), rabbit anti-RAB3GAP1 (Proteintech, Manchester, UK; 21663-1-AP), rabbit anti-RAB3GAP2 (Abgent, Maidenhead, UK; AP9635B), rabbit anti-WDR44 (Bethyl, Montgomery, USA; A301-441A), mouse anti-ASNA1 (Abnova, H00000439-M03), rabbit anti-Syntaxin 1A (GeneTex, Irvine, USA; GTX113559), rabbit anti-BAG6 (Cell Signaling, 8523S), mouse anti-RPN2 (Abnova, H00006185-B01), rabbit anti-CD147 (Abcam, Cambridge, UK; ab108317), Alexa Fluor® 488 goat anti-rabbit (Invitrogen, A11008) and Alexa Fluor® 594 chicken anti-mouse (Invitrogen, A21201).

    Techniques:

    ASNA1 interacts with VAPB via a FFAT-like motif similar to FAF1. (A) Alignment of the FFAT-like motifs in human ASNA1 and FAF1. (B) Alignment of the FFAT-like motif of ASNA1 across species showing that it is highly conserved. (C) A point mutation in the FFAT-like motif of ASNA1 (F15A) abolishes its interaction with VAPB. WT and mutant Flag-ASNA1 were immunoprecipitated from U2OS cells using anti-Flag beads. (D) Indirect immunofluorescence of VAPB and Flag-ASNA1 WT. U2OS cells were transfected with Flag-ASNA1 WT for 24 hr. Flag-ASNA1 WT (red) is co-localized with VAPB (green) in a peri-nuclear area (enlarged window) suggesting an ER pattern. Scale bar is 10 μm. (E) ASNA1 interaction with FAF1 is strongly stimulated upon proteasome inhibition with MG132 and depends on the UBA domain. WT Flag-FAF1 and the indicated mutants were immunoprecipitated from U2OS cells. (F) G46R and G46A point mutations in ASNA1 abolish its interaction with BAG6 and strongly reduce its interaction with FAF1 and ubiquitin, most noticeably after MG132 treatment, but do not affect the interaction with VAPB. WT and mutant Flag-ASNA1 were immunoprecipitated from SH-SY5Y cells. DAPI, 4',6-diamidino-2-phenylindole; IP, immunoprecipitate; WT, wild type.

    Journal: BMC Biology

    Article Title: VAPB/ALS8 interacts with FFAT-like proteins including the p97 cofactor FAF1 and the ASNA1 ATPase

    doi: 10.1186/1741-7007-12-39

    Figure Lengend Snippet: ASNA1 interacts with VAPB via a FFAT-like motif similar to FAF1. (A) Alignment of the FFAT-like motifs in human ASNA1 and FAF1. (B) Alignment of the FFAT-like motif of ASNA1 across species showing that it is highly conserved. (C) A point mutation in the FFAT-like motif of ASNA1 (F15A) abolishes its interaction with VAPB. WT and mutant Flag-ASNA1 were immunoprecipitated from U2OS cells using anti-Flag beads. (D) Indirect immunofluorescence of VAPB and Flag-ASNA1 WT. U2OS cells were transfected with Flag-ASNA1 WT for 24 hr. Flag-ASNA1 WT (red) is co-localized with VAPB (green) in a peri-nuclear area (enlarged window) suggesting an ER pattern. Scale bar is 10 μm. (E) ASNA1 interaction with FAF1 is strongly stimulated upon proteasome inhibition with MG132 and depends on the UBA domain. WT Flag-FAF1 and the indicated mutants were immunoprecipitated from U2OS cells. (F) G46R and G46A point mutations in ASNA1 abolish its interaction with BAG6 and strongly reduce its interaction with FAF1 and ubiquitin, most noticeably after MG132 treatment, but do not affect the interaction with VAPB. WT and mutant Flag-ASNA1 were immunoprecipitated from SH-SY5Y cells. DAPI, 4',6-diamidino-2-phenylindole; IP, immunoprecipitate; WT, wild type.

    Article Snippet: The following antibodies were used: mouse anti-Flag M2 (Sigma, A8592), mouse anti-ubiquitin FK2 (Enzo, PW8810), rabbit anti-ubiquitin (Dako, Ely, UK; Z0458), mouse anti-p97 (Fitzgerald, North Acton, USA; 10R-P104A), rabbit anti-VAPA (Epitomics, Burlingame, USA; S1706), mouse anti-FAF1 (Abnova, Taipei City, Taiwan; H00011124-A01), rabbit anti-FAF1 (courtesy of Millipore, Billerica, USA), rabbit anti-GAPDH (Cell Signaling, 2118), rabbit anti-RAB3GAP1 (Proteintech, Manchester, UK; 21663-1-AP), rabbit anti-RAB3GAP2 (Abgent, Maidenhead, UK; AP9635B), rabbit anti-WDR44 (Bethyl, Montgomery, USA; A301-441A), mouse anti-ASNA1 (Abnova, H00000439-M03), rabbit anti-Syntaxin 1A (GeneTex, Irvine, USA; GTX113559), rabbit anti-BAG6 (Cell Signaling, 8523S), mouse anti-RPN2 (Abnova, H00006185-B01), rabbit anti-CD147 (Abcam, Cambridge, UK; ab108317), Alexa Fluor® 488 goat anti-rabbit (Invitrogen, A11008) and Alexa Fluor® 594 chicken anti-mouse (Invitrogen, A21201).

    Techniques: Mutagenesis, Immunoprecipitation, Immunofluorescence, Transfection, Inhibition

    PERM1 is a novel transcription coactivator that functionally interacts with PGC-1α, BAG6, and KANK2. (A) Immunoprecipitation assays show that PERM1 binds to the transcriptional regulators ERRα, PGC-1α, ANKRD1, BAG6, KANK2, and TIF1β. Adenovirus Flag-tagged Perm1 (PERM1-Flag) was transduced to cardiomyocytes, and PERM1-bound proteins were pulled down by anti-Flag antibody. Immunoblotting confirmed the interaction of PERM1 with ERRα, PGC-1α, ANKRD1, BAG6, KANK2, and TIF1β. In contrast, TRX1, which was also identified through MS-based screening as a potential binding partner in transcription regulation, did not bind to PERM1. (B) Luciferase reporter gene assays show that the PERM1-induced transcriptional activation of the ERRE requires PGC-1α, BAG6, and KANK2 ( n = 7-9/group). Cardiomyocytes were transduced with 3xERRE-luc, followed by transfecting with either scrambled-siRNA (scr), siPGC-1α, siANKRD1, siBAG6, siKANK2, or TIF1β. (C) In vitro Gal4 assay shows the recruitment of PERM1 to a gene promoter induces transcriptional activation ( n = 6/group). Gal4-fused Perm1 (Gal4- Perm1 ) was expressed with UAS-luc, a reporter gene driven by Gal4 binding sequence, in cardiomyocytes. In control (scrambled-siRNA, “scr”), the reporter activity was significantly increased by Gal4- Perm1 , indicating that PERM1 can act as a transcription coactivator. Silencing of PGC-1α, BAG6, KANK2 inhibited the transcription activation by PERM1. (D) qPCR shows downregulation of ERR target genes by silencing BAG6 and KANK2 (siBag6 and siKank2) in cultured cardiomyocytes ( n = 4/group). (E) siRNA-mediated knockdown of PGC-1α, ANKRD1, BAG6, KANK2, or TIF1β were verified by western blotting analyses. (F) Hypothetical model of transcriptional regulation by PERM1 on the ERRE. PERM1 is localized to and activates the ERRE in ERR target genes through interacting with ERRα and the other transcriptional regulators BAG6, KANK2, and PGC-1α (* p < 0.05).

    Journal: Frontiers in Cardiovascular Medicine

    Article Title: PERM1 regulates energy metabolism in the heart via ERRα/PGC−1α axis

    doi: 10.3389/fcvm.2022.1033457

    Figure Lengend Snippet: PERM1 is a novel transcription coactivator that functionally interacts with PGC-1α, BAG6, and KANK2. (A) Immunoprecipitation assays show that PERM1 binds to the transcriptional regulators ERRα, PGC-1α, ANKRD1, BAG6, KANK2, and TIF1β. Adenovirus Flag-tagged Perm1 (PERM1-Flag) was transduced to cardiomyocytes, and PERM1-bound proteins were pulled down by anti-Flag antibody. Immunoblotting confirmed the interaction of PERM1 with ERRα, PGC-1α, ANKRD1, BAG6, KANK2, and TIF1β. In contrast, TRX1, which was also identified through MS-based screening as a potential binding partner in transcription regulation, did not bind to PERM1. (B) Luciferase reporter gene assays show that the PERM1-induced transcriptional activation of the ERRE requires PGC-1α, BAG6, and KANK2 ( n = 7-9/group). Cardiomyocytes were transduced with 3xERRE-luc, followed by transfecting with either scrambled-siRNA (scr), siPGC-1α, siANKRD1, siBAG6, siKANK2, or TIF1β. (C) In vitro Gal4 assay shows the recruitment of PERM1 to a gene promoter induces transcriptional activation ( n = 6/group). Gal4-fused Perm1 (Gal4- Perm1 ) was expressed with UAS-luc, a reporter gene driven by Gal4 binding sequence, in cardiomyocytes. In control (scrambled-siRNA, “scr”), the reporter activity was significantly increased by Gal4- Perm1 , indicating that PERM1 can act as a transcription coactivator. Silencing of PGC-1α, BAG6, KANK2 inhibited the transcription activation by PERM1. (D) qPCR shows downregulation of ERR target genes by silencing BAG6 and KANK2 (siBag6 and siKank2) in cultured cardiomyocytes ( n = 4/group). (E) siRNA-mediated knockdown of PGC-1α, ANKRD1, BAG6, KANK2, or TIF1β were verified by western blotting analyses. (F) Hypothetical model of transcriptional regulation by PERM1 on the ERRE. PERM1 is localized to and activates the ERRE in ERR target genes through interacting with ERRα and the other transcriptional regulators BAG6, KANK2, and PGC-1α (* p < 0.05).

    Article Snippet: These denatured protein samples were transferred to either polyvinylidene difluoride or nitrocellulose membranes and probed with antibodies against Perm1 (Sigma HPA032711), ERRα (Millipore ERR46Y), PGC-1α (Millipore Ab3242), Ankrd1 (Novus NBP2-15397), BAG6 (Cell Signaling Technology 8523), Kank2 (Novus NBP3-04645), TIF1b (Cell Signaling Technology 4123), and Trx1 (Cell Signaling Technology 2429).

    Techniques: Immunoprecipitation, Western Blot, Binding Assay, Luciferase, Activation Assay, Transduction, In Vitro, Sequencing, Activity Assay, Cell Culture

    The RBULs link posttranscriptional processes to the ubiquitin system. ( a ) The BP and MF GO terms of the interactors of the six RBULs were grouped into the categories “RNA” (blue), “Ubiquitin” (turquoise), and “Other” (rose). The distribution of the categories among the interactomes is shown. ( b ) A summary of GO terms for MEX3B interaction partners is shown. ( c , d ) Validation of RBUL interaction partners by pulldowns and Western blot. ( c ) Endogenous PRPF19 was pulled down with a PRPF19-specific antibody from HEK293T cells. Experiments omitting the antibody served as control. Western blot analysis was performed with antibodies specific against BAG2, BAG6, VCP, and HSPA1A, as well as against PRPF19 itself to validate the immunoprecipitation (IP). Left: Cropped images of input and IP samples (replicate 1). Images of full membranes and different exposure times for all antibodies and replicates are presented in Supplementary Figure . Right: Quantifications of the PRPF19-specific IPs normalized to control of three independent biological replicates are shown in a dot plot, including mean and standard error (s.e.m.). ( d ) GFP (empty vector, EV) and GFP-MEX3B were expressed in HEK293T cells and pulled down with a GFP-specific antibody. Western blot analysis was performed using specific antibodies against POLR1A, POLR3A, VCP, and HSPA1A, as well as GFP. Left: Cropped images of input and AP samples (replicate 1). Images of full membranes and different exposure times for all antibodies are presented in Supplementary Figure . Right: Quantification of the APs normalized to EV are shown as in ( c ).

    Journal: Scientific Reports

    Article Title: Interaction profiling of RNA-binding ubiquitin ligases reveals a link between posttranscriptional regulation and the ubiquitin system

    doi: 10.1038/s41598-017-16695-6

    Figure Lengend Snippet: The RBULs link posttranscriptional processes to the ubiquitin system. ( a ) The BP and MF GO terms of the interactors of the six RBULs were grouped into the categories “RNA” (blue), “Ubiquitin” (turquoise), and “Other” (rose). The distribution of the categories among the interactomes is shown. ( b ) A summary of GO terms for MEX3B interaction partners is shown. ( c , d ) Validation of RBUL interaction partners by pulldowns and Western blot. ( c ) Endogenous PRPF19 was pulled down with a PRPF19-specific antibody from HEK293T cells. Experiments omitting the antibody served as control. Western blot analysis was performed with antibodies specific against BAG2, BAG6, VCP, and HSPA1A, as well as against PRPF19 itself to validate the immunoprecipitation (IP). Left: Cropped images of input and IP samples (replicate 1). Images of full membranes and different exposure times for all antibodies and replicates are presented in Supplementary Figure . Right: Quantifications of the PRPF19-specific IPs normalized to control of three independent biological replicates are shown in a dot plot, including mean and standard error (s.e.m.). ( d ) GFP (empty vector, EV) and GFP-MEX3B were expressed in HEK293T cells and pulled down with a GFP-specific antibody. Western blot analysis was performed using specific antibodies against POLR1A, POLR3A, VCP, and HSPA1A, as well as GFP. Left: Cropped images of input and AP samples (replicate 1). Images of full membranes and different exposure times for all antibodies are presented in Supplementary Figure . Right: Quantification of the APs normalized to EV are shown as in ( c ).

    Article Snippet: The following antibodies were used: anti-GFP (B-2 clone; Santa Cruz; sc-9996), anti-HSP70 (Enzo Life Sciences; N15F2-5), anti-BAG6 (Cell Signaling Technology, 8523), anti-VCP (Cell Signaling Technology; 2649), anti-BAG2 (Sigma Alrich; HPA018862), anti-PRPF19 (Abcam; ab27692), anti-POLR1A (Santa Cruz; sc-48385), anti-POLR3A (D5Y2D; Cell Signaling Technology, 12825).

    Techniques: Western Blot, Immunoprecipitation, Plasmid Preparation