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anti ha rabbit y11 antibodies  (Santa Cruz Biotechnology)


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    Santa Cruz Biotechnology anti ha rabbit y11 antibodies
    Fig. 1. PML induced by IFNα suppresses intrinsic telomerase activities in H1299 cells. (A) Ablation of endogenous PML under IFNα treatment. H1299 cell lines were treated with 1000 U/ml IFNα in the presence of control or 200 nM PML siRNA. The levels of PML and actin in cell extracts harvested at indicated times were subjected to immunoblotting using anti-PML and anti-actin antibodies. The cell extracts (30 ng) were added for TRAP analyses. NC and PC denote negative control and positive control, respectively. TRAP analysis for NC was performed in the absence of cell extracts. The 36 bp represents the internal TRAP assay standards. The ImageJ (NIH) program was used to measure the relative amounts of bands in the TRAP assays after normalizing to 36 bp band, and are shown in the panel on the right. (B) Detection of the TERT mRNA levels. The mRNA of the cells treated with control or PML siRNA in the presence or absence of IFNα was extracted and tested for the levels of TERT mRNA using RT-PCR. The mRNA levels of GAPDH were analyzed as a control. (C) Co-localization of TERT-HA with PML-NBs. H1299 cells were transfected with plasmid expressing TERT-HA with or without IFNα. Cells were fixed after 24 hours and analyzed by immunofluorescence with <t>anti-HA</t> and anti-PML antibodies followed by Alexa Fluor 594 rabbit (red) and Alexa Fluor 488 mouse (green) secondary antibodies. A fluorescent microscope was used to detect the proteins, with a total of 200 cells counted for each experiment. DAPI was used to visualize the nuclei. Cells displaying colocalization of TERT and PML-NBs were counted and shown as graph on right. Cells were captured with the same exposure times (200 milliseconds for TERT, 800 milliseconds for PML). (D) Immunoprecipitation of TERT-HA with endogenous PML. Plasmid expressing TERT-HA was transfected into untreated or IFNα-treated H1299 cells. Whole cell lysates (WCLs) were immunoprecipitated with anti-HA antibodies and immunoblotted with anti-PML, anti-HA and anti- actin antibodies. Cell lysates (5% or 20%) used for immunoprecipitation were subjected to Western blot as an input.
    Anti Ha Rabbit Y11 Antibodies, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 5818 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/trapz+function/pm19567472-302-8-15?v=Santa+Cruz+Biotechnology
    Average 96 stars, based on 5818 article reviews
    anti ha rabbit y11 antibodies - by Bioz Stars, 2026-08
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    1) Product Images from "PML-IV functions as a negative regulator of telomerase by interacting with TERT."

    Article Title: PML-IV functions as a negative regulator of telomerase by interacting with TERT.

    Journal: Journal of cell science

    doi: 10.1242/jcs.048066

    Fig. 1. PML induced by IFNα suppresses intrinsic telomerase activities in H1299 cells. (A) Ablation of endogenous PML under IFNα treatment. H1299 cell lines were treated with 1000 U/ml IFNα in the presence of control or 200 nM PML siRNA. The levels of PML and actin in cell extracts harvested at indicated times were subjected to immunoblotting using anti-PML and anti-actin antibodies. The cell extracts (30 ng) were added for TRAP analyses. NC and PC denote negative control and positive control, respectively. TRAP analysis for NC was performed in the absence of cell extracts. The 36 bp represents the internal TRAP assay standards. The ImageJ (NIH) program was used to measure the relative amounts of bands in the TRAP assays after normalizing to 36 bp band, and are shown in the panel on the right. (B) Detection of the TERT mRNA levels. The mRNA of the cells treated with control or PML siRNA in the presence or absence of IFNα was extracted and tested for the levels of TERT mRNA using RT-PCR. The mRNA levels of GAPDH were analyzed as a control. (C) Co-localization of TERT-HA with PML-NBs. H1299 cells were transfected with plasmid expressing TERT-HA with or without IFNα. Cells were fixed after 24 hours and analyzed by immunofluorescence with anti-HA and anti-PML antibodies followed by Alexa Fluor 594 rabbit (red) and Alexa Fluor 488 mouse (green) secondary antibodies. A fluorescent microscope was used to detect the proteins, with a total of 200 cells counted for each experiment. DAPI was used to visualize the nuclei. Cells displaying colocalization of TERT and PML-NBs were counted and shown as graph on right. Cells were captured with the same exposure times (200 milliseconds for TERT, 800 milliseconds for PML). (D) Immunoprecipitation of TERT-HA with endogenous PML. Plasmid expressing TERT-HA was transfected into untreated or IFNα-treated H1299 cells. Whole cell lysates (WCLs) were immunoprecipitated with anti-HA antibodies and immunoblotted with anti-PML, anti-HA and anti- actin antibodies. Cell lysates (5% or 20%) used for immunoprecipitation were subjected to Western blot as an input.
    Figure Legend Snippet: Fig. 1. PML induced by IFNα suppresses intrinsic telomerase activities in H1299 cells. (A) Ablation of endogenous PML under IFNα treatment. H1299 cell lines were treated with 1000 U/ml IFNα in the presence of control or 200 nM PML siRNA. The levels of PML and actin in cell extracts harvested at indicated times were subjected to immunoblotting using anti-PML and anti-actin antibodies. The cell extracts (30 ng) were added for TRAP analyses. NC and PC denote negative control and positive control, respectively. TRAP analysis for NC was performed in the absence of cell extracts. The 36 bp represents the internal TRAP assay standards. The ImageJ (NIH) program was used to measure the relative amounts of bands in the TRAP assays after normalizing to 36 bp band, and are shown in the panel on the right. (B) Detection of the TERT mRNA levels. The mRNA of the cells treated with control or PML siRNA in the presence or absence of IFNα was extracted and tested for the levels of TERT mRNA using RT-PCR. The mRNA levels of GAPDH were analyzed as a control. (C) Co-localization of TERT-HA with PML-NBs. H1299 cells were transfected with plasmid expressing TERT-HA with or without IFNα. Cells were fixed after 24 hours and analyzed by immunofluorescence with anti-HA and anti-PML antibodies followed by Alexa Fluor 594 rabbit (red) and Alexa Fluor 488 mouse (green) secondary antibodies. A fluorescent microscope was used to detect the proteins, with a total of 200 cells counted for each experiment. DAPI was used to visualize the nuclei. Cells displaying colocalization of TERT and PML-NBs were counted and shown as graph on right. Cells were captured with the same exposure times (200 milliseconds for TERT, 800 milliseconds for PML). (D) Immunoprecipitation of TERT-HA with endogenous PML. Plasmid expressing TERT-HA was transfected into untreated or IFNα-treated H1299 cells. Whole cell lysates (WCLs) were immunoprecipitated with anti-HA antibodies and immunoblotted with anti-PML, anti-HA and anti- actin antibodies. Cell lysates (5% or 20%) used for immunoprecipitation were subjected to Western blot as an input.

    Techniques Used: Control, Western Blot, Negative Control, Positive Control, TRAP Assay, Reverse Transcription Polymerase Chain Reaction, Transfection, Plasmid Preparation, Expressing, Immunofluorescence, Microscopy, Immunoprecipitation

    Fig. 2. PML-IV interacts specifically with TERT. (A) Schematic view of the six PML isoforms. (B) The interaction between TERT and PML isoforms. Six FLAG- PML isoforms (I-IV) were transfected into HEK293T cells along with TERT-HA. Whole cell lysates were immunoprecipitated with anti-FLAG antibodies. FLAG immunoprecipitates and 20% input were loaded and immunoblotting was performed using anti-HA and anti-FLAG. (C) Co- localization of TERT with PML-IV. H1299 cells were co-transfected with plasmids expressing TERT-HA and FLAG-PML isoforms. Cells were fixed after 24 hours and analyzed by immunofluorescence using anti-HA and anti-FLAG antibodies followed by Alexa Fluor 594 rabbit (red) and Alexa Fluor 488 mouse (green) secondary antibodies. Nuclei were visualized by DAPI staining.
    Figure Legend Snippet: Fig. 2. PML-IV interacts specifically with TERT. (A) Schematic view of the six PML isoforms. (B) The interaction between TERT and PML isoforms. Six FLAG- PML isoforms (I-IV) were transfected into HEK293T cells along with TERT-HA. Whole cell lysates were immunoprecipitated with anti-FLAG antibodies. FLAG immunoprecipitates and 20% input were loaded and immunoblotting was performed using anti-HA and anti-FLAG. (C) Co- localization of TERT with PML-IV. H1299 cells were co-transfected with plasmids expressing TERT-HA and FLAG-PML isoforms. Cells were fixed after 24 hours and analyzed by immunofluorescence using anti-HA and anti-FLAG antibodies followed by Alexa Fluor 594 rabbit (red) and Alexa Fluor 488 mouse (green) secondary antibodies. Nuclei were visualized by DAPI staining.

    Techniques Used: Transfection, Immunoprecipitation, Western Blot, Expressing, Immunofluorescence, Staining

    Fig. 3. The C-terminal region of PML-IV is required for TERT recruitment. (A) Schematic representation of various PML mutants showing their functional domains. (B) Interaction between TERT and C-terminal deletion PML mutants. Expression plasmids for TERT-HA and/or FLAG-tagged C-terminal deletion mutants of PML-IV were transfected into HEK293T cells. 24 hours after transfection, whole cell lysates were immunoprecipitated with anti-FLAG antibodies and assayed by immunoblotting with anti-HA and anti-FLAG antibodies. (C) Interaction between TERT and PML mutants. Plasmids expressing wild-type or truncated PML mutants and/or TERT-HA were transfected into HEK293T cells. Whole cell lysates were immunoprecipitated with anti-FLAG antibodies. Immunoblotting was performed with anti-HA and anti-FLAG antibodies. (D) Interaction between PML3M and TERT. Plasmids expressing TERT-HA, FLAG-PML-IV, or FLAG- PML3M were transfected into HEK293T cells. Whole cell lysates were subjected to immunoprecipitation using anti-FLAG antibodies followed by western blotting using anti-HA and anti-FLAG antibodies. (E) The interaction between TERT and the C-terminal fragment of PML-IV. Plasmids expressing TERT-HA, Myc-PML- IV, Myc-553-633 or Myc-571-633 were transfected into HEK293T cells. Whole cell lysates were subjected to immunoprecipitation using anti-Myc antibodies followed by western blotting using anti-HA and anti-Myc antibodies. The asterisks indicate heavy and light chains. pCS3-MT-BX empty vector produces 25 kDa polypeptide consisting of 6Myc epitope (lane 2). In the immunoprecipitation analysis (B-E), 20% of lysates were used as an input.
    Figure Legend Snippet: Fig. 3. The C-terminal region of PML-IV is required for TERT recruitment. (A) Schematic representation of various PML mutants showing their functional domains. (B) Interaction between TERT and C-terminal deletion PML mutants. Expression plasmids for TERT-HA and/or FLAG-tagged C-terminal deletion mutants of PML-IV were transfected into HEK293T cells. 24 hours after transfection, whole cell lysates were immunoprecipitated with anti-FLAG antibodies and assayed by immunoblotting with anti-HA and anti-FLAG antibodies. (C) Interaction between TERT and PML mutants. Plasmids expressing wild-type or truncated PML mutants and/or TERT-HA were transfected into HEK293T cells. Whole cell lysates were immunoprecipitated with anti-FLAG antibodies. Immunoblotting was performed with anti-HA and anti-FLAG antibodies. (D) Interaction between PML3M and TERT. Plasmids expressing TERT-HA, FLAG-PML-IV, or FLAG- PML3M were transfected into HEK293T cells. Whole cell lysates were subjected to immunoprecipitation using anti-FLAG antibodies followed by western blotting using anti-HA and anti-FLAG antibodies. (E) The interaction between TERT and the C-terminal fragment of PML-IV. Plasmids expressing TERT-HA, Myc-PML- IV, Myc-553-633 or Myc-571-633 were transfected into HEK293T cells. Whole cell lysates were subjected to immunoprecipitation using anti-Myc antibodies followed by western blotting using anti-HA and anti-Myc antibodies. The asterisks indicate heavy and light chains. pCS3-MT-BX empty vector produces 25 kDa polypeptide consisting of 6Myc epitope (lane 2). In the immunoprecipitation analysis (B-E), 20% of lysates were used as an input.

    Techniques Used: Functional Assay, Expressing, Transfection, Immunoprecipitation, Western Blot, Plasmid Preparation

    Fig. 4. Deletion fragments of TERT localize to the nucleoplasm in speckles. (A) Schematic representation of the TERT deletion constructs used in this study (Autexier and Lue, 2006; Xia et al., 2000). (B) Subcellular localization of TERT and its deletion constructs. H1299 cells were transfected with plasmids expressing TERT or the TERT fragments. 24 hours after transfection, cells were lysed and immunoblotted using anti-HA-rabbit antibodies (right panel). H1299 cells were transfected with plasmids expressing TERT-HA or its deletion mutants. The expressed proteins were detected with anti-HA antibodies followed by Alexa Fluor 594 rabbit (red) secondary antibodies. (C) Colocalization of TERT or its deletion mutants with PML-NBs. H1299 cells were co-transfected with expression vector for TERT-HA (panels 1-4) or its mutants (panels 5-20). Cells were fixed and detected using anti-HA and anti-PML antibodies followed by Alexa Fluor 594 rabbit (red) and Alexa Fluor 488 mouse (green) secondary antibodies. Transfected cells were analyzed using confocal microscopy. Endo PML, endogenous PML; PC, phase contrast. A total of 100 cells were counted for each experiment.
    Figure Legend Snippet: Fig. 4. Deletion fragments of TERT localize to the nucleoplasm in speckles. (A) Schematic representation of the TERT deletion constructs used in this study (Autexier and Lue, 2006; Xia et al., 2000). (B) Subcellular localization of TERT and its deletion constructs. H1299 cells were transfected with plasmids expressing TERT or the TERT fragments. 24 hours after transfection, cells were lysed and immunoblotted using anti-HA-rabbit antibodies (right panel). H1299 cells were transfected with plasmids expressing TERT-HA or its deletion mutants. The expressed proteins were detected with anti-HA antibodies followed by Alexa Fluor 594 rabbit (red) secondary antibodies. (C) Colocalization of TERT or its deletion mutants with PML-NBs. H1299 cells were co-transfected with expression vector for TERT-HA (panels 1-4) or its mutants (panels 5-20). Cells were fixed and detected using anti-HA and anti-PML antibodies followed by Alexa Fluor 594 rabbit (red) and Alexa Fluor 488 mouse (green) secondary antibodies. Transfected cells were analyzed using confocal microscopy. Endo PML, endogenous PML; PC, phase contrast. A total of 100 cells were counted for each experiment.

    Techniques Used: Construct, Transfection, Expressing, Plasmid Preparation, Confocal Microscopy

    Fig. 5. Two regions of TERT, 1-350 and 595-946, are required for TERT interaction with PML-IV. (A) Interaction between PML-IV and TERT. To detect the interaction between TERT and PML-IV, HEK293T cells were transfected with expression plasmids for TERT-HA and/or FLAG-PML-IV. Immunoprecipitation analyses were carried out as indicated in Fig. 2B. (B) The interaction between TERT fragments and PML-IV. To analyze the binding domain of TERT, HEK293T cells were transfected with expression plasmids for FLAG-PML-IV and/or HA-TERT mutants. Cell lysates were immunoprecipitated as described above using anti-HA antibodies and immunoblotted using anti-HA and anti-FLAG antibodies. (C) Interaction between TERT fragments and PML-IV 553-633 fragment. To analyze the binding domain between TERT and PML-IV, HEK293T cells were transfected with expression plasmids for FLAG-PML-IV (553-633) and/or HA- TERT mutants. Immunoprecipitations were carried out as described above. Immunoblotting was performed using anti-Myc and anti-HA antibodies. (D) Co- localization of TERT or its deletion mutants with PML-IV. H1299 cells were cotransfected with expression plasmids for TERT-HA (panels 1-4) or its mutants (panels 5-20) with FLAG-PML-IV. Cells were fixed and detected using anti-HA and anti-FLAG antibodies followed by Alexa Fluor 594 rabbit (Red) and Alexa Fluor 488 mouse (Green) secondary antibodies. Transfected cells were analyzed as described n Fig. 2C. A total of 100 cells were counted for each experiment. Cells were captured with the same exposure times (200 milliseconds for TERT, 800 milliseconds for PML).
    Figure Legend Snippet: Fig. 5. Two regions of TERT, 1-350 and 595-946, are required for TERT interaction with PML-IV. (A) Interaction between PML-IV and TERT. To detect the interaction between TERT and PML-IV, HEK293T cells were transfected with expression plasmids for TERT-HA and/or FLAG-PML-IV. Immunoprecipitation analyses were carried out as indicated in Fig. 2B. (B) The interaction between TERT fragments and PML-IV. To analyze the binding domain of TERT, HEK293T cells were transfected with expression plasmids for FLAG-PML-IV and/or HA-TERT mutants. Cell lysates were immunoprecipitated as described above using anti-HA antibodies and immunoblotted using anti-HA and anti-FLAG antibodies. (C) Interaction between TERT fragments and PML-IV 553-633 fragment. To analyze the binding domain between TERT and PML-IV, HEK293T cells were transfected with expression plasmids for FLAG-PML-IV (553-633) and/or HA- TERT mutants. Immunoprecipitations were carried out as described above. Immunoblotting was performed using anti-Myc and anti-HA antibodies. (D) Co- localization of TERT or its deletion mutants with PML-IV. H1299 cells were cotransfected with expression plasmids for TERT-HA (panels 1-4) or its mutants (panels 5-20) with FLAG-PML-IV. Cells were fixed and detected using anti-HA and anti-FLAG antibodies followed by Alexa Fluor 594 rabbit (Red) and Alexa Fluor 488 mouse (Green) secondary antibodies. Transfected cells were analyzed as described n Fig. 2C. A total of 100 cells were counted for each experiment. Cells were captured with the same exposure times (200 milliseconds for TERT, 800 milliseconds for PML).

    Techniques Used: Transfection, Expressing, Immunoprecipitation, Binding Assay, Western Blot

    Fig. 6. PML-IV negatively regulates telomerase activity in H1299 cells. (A) The effect of PML-IV on telomerase activity. H1299 cells were transfected with either empty vector or the plasmids expressing FLAG-PML-IV. Increasing concentrations of cell extracts (10, 30 and 50 ng) were added for TRAP analyses as described in Fig. 1A. (B) The effects of PML isoforms on telomerase activities. H1299 cells were transfected with the empty plasmid or the vectors expressing PML I-IV (upper panel). The extracts from the transfected cells (30 ng) were tested for telomerase activities and subjected to immunoblotting using anti-FLAG and anti-actin antibodies. (C) The effects of PML C-terminal fragment on telomerase activities. H1299 cells were transfected with the vectors expressing 6Myc epitope (control vector), Myc-PML-IV, Myc-553-633 or Myc-571-633 (upper panel). The extracts from the transfected cells (30 ng) were tested for telomerase activity and subjected to immunoblotting using anti-Myc and anti-actin antibodies. (D) Detection of the TERT mRNA levels. H1299 cells transfected with expression vectors for Myc-PML-IV, Myc-553-633 or Myc-571-633. After RNA extraction from transfected cells, mRNA levels of TERT were measured by RT-PCR. The mRNA levels of GAPDH were analyzed as a control. (E) Telomerase activity of the immunoprecipitated TERT by PML-IV and its 553-633 deletion mutant. Plasmids expressing FLAG-Ku70, FLAG-PML-IV, Myc-PML-IV, Myc-553-633, or empty vectors were transfected into HEK293T cells with expression vector for TERT- HA. Whole cell lysates were subjected to immunoblotting with anti-HA, anti-FLAG and anti-Myc antibodies (lanes 1-6). The lysates were immunoprecipitated with anti-FLAG or anti-Myc antibodies and assayed by immunoblotting with anti-HA antibodies (lanes 7-12) to detect TERT. 5% of the immunoprecipitated sample was analyzed for telomerase activity using a TRAP assay.
    Figure Legend Snippet: Fig. 6. PML-IV negatively regulates telomerase activity in H1299 cells. (A) The effect of PML-IV on telomerase activity. H1299 cells were transfected with either empty vector or the plasmids expressing FLAG-PML-IV. Increasing concentrations of cell extracts (10, 30 and 50 ng) were added for TRAP analyses as described in Fig. 1A. (B) The effects of PML isoforms on telomerase activities. H1299 cells were transfected with the empty plasmid or the vectors expressing PML I-IV (upper panel). The extracts from the transfected cells (30 ng) were tested for telomerase activities and subjected to immunoblotting using anti-FLAG and anti-actin antibodies. (C) The effects of PML C-terminal fragment on telomerase activities. H1299 cells were transfected with the vectors expressing 6Myc epitope (control vector), Myc-PML-IV, Myc-553-633 or Myc-571-633 (upper panel). The extracts from the transfected cells (30 ng) were tested for telomerase activity and subjected to immunoblotting using anti-Myc and anti-actin antibodies. (D) Detection of the TERT mRNA levels. H1299 cells transfected with expression vectors for Myc-PML-IV, Myc-553-633 or Myc-571-633. After RNA extraction from transfected cells, mRNA levels of TERT were measured by RT-PCR. The mRNA levels of GAPDH were analyzed as a control. (E) Telomerase activity of the immunoprecipitated TERT by PML-IV and its 553-633 deletion mutant. Plasmids expressing FLAG-Ku70, FLAG-PML-IV, Myc-PML-IV, Myc-553-633, or empty vectors were transfected into HEK293T cells with expression vector for TERT- HA. Whole cell lysates were subjected to immunoblotting with anti-HA, anti-FLAG and anti-Myc antibodies (lanes 1-6). The lysates were immunoprecipitated with anti-FLAG or anti-Myc antibodies and assayed by immunoblotting with anti-HA antibodies (lanes 7-12) to detect TERT. 5% of the immunoprecipitated sample was analyzed for telomerase activity using a TRAP assay.

    Techniques Used: Activity Assay, Transfection, Plasmid Preparation, Expressing, Western Blot, Control, RNA Extraction, Reverse Transcription Polymerase Chain Reaction, Immunoprecipitation, Mutagenesis, TRAP Assay

    Fig. 7. H1299 stable cell lines overexpressing PML-IV suppress TERT activity. (A) FLAG-PML-IV expression in PML stable cell lines. PML- IV, expressed in PML-IV-stable cell lines, was detected using anti-PML or anti-HA antibodies. H1299 cell lines stably transfected with pCMV- Tag2B (mock) were also tested using the same antibodies. The asterisk indicates stably overexpressed FLAG-PML-IV. (B) Detection of the TERT mRNA and hTERC levels in the stable cell lines. The RNA of the stable cell lines was extracted and tested for the TERT mRNA or hTERC using RT-PCR as described in Fig. 1. The mRNA levels of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) were tested as a control. (C) Telomerase activity of the PML-IV-stable cell lines. The extracts of H1299, mock, or stable cell lines were tested for telomerase activity as described in Fig. 5. (D) Detection of telomere length in stable cell lines. The telomere length of the cell lines used above was determined by TRF analyses. The mock cell line was used as a control.
    Figure Legend Snippet: Fig. 7. H1299 stable cell lines overexpressing PML-IV suppress TERT activity. (A) FLAG-PML-IV expression in PML stable cell lines. PML- IV, expressed in PML-IV-stable cell lines, was detected using anti-PML or anti-HA antibodies. H1299 cell lines stably transfected with pCMV- Tag2B (mock) were also tested using the same antibodies. The asterisk indicates stably overexpressed FLAG-PML-IV. (B) Detection of the TERT mRNA and hTERC levels in the stable cell lines. The RNA of the stable cell lines was extracted and tested for the TERT mRNA or hTERC using RT-PCR as described in Fig. 1. The mRNA levels of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) were tested as a control. (C) Telomerase activity of the PML-IV-stable cell lines. The extracts of H1299, mock, or stable cell lines were tested for telomerase activity as described in Fig. 5. (D) Detection of telomere length in stable cell lines. The telomere length of the cell lines used above was determined by TRF analyses. The mock cell line was used as a control.

    Techniques Used: Stable Transfection, Activity Assay, Expressing, Transfection, Reverse Transcription Polymerase Chain Reaction, Control



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