Review



rabbit anti trf2  (Novus Biologicals)


Bioz Verified Symbol Novus Biologicals is a verified supplier
Bioz Manufacturer Symbol Novus Biologicals manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 95

    Structured Review

    Novus Biologicals rabbit anti trf2
    Rabbit Anti Trf2, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 95/100, based on 124 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+trf2/pm41712379-430-4-5?v=Novus+Biologicals
    Average 95 stars, based on 124 article reviews
    rabbit anti trf2 - by Bioz Stars, 2026-07
    95/100 stars

    Images



    Similar Products

    93
    Cell Signaling Technology Inc trf2 antibody
    Effect of DISS on telomere. ( A ) The changes in telomerase content after treatment with 0, 1, 3, 10 μM DISS or 10 μM RES. ( B ) Relative telomere length of 3T3 cells after treatment with 0, 1, 3, 10 μM DISS or 10 μM AST. ( C , D ) Effects of 1, 3, 10 μM DISS or 10 μM RES on EST1 , EST2 genes at 24 and 48 h. ( E ) Effects of 0, 1, 3, 10 μM DISS or 10 μM AST on <t>TRF2</t> protein expressions and digital results. ( F ) Effects of 0, 1, 3, 10 μM DISS or 10 μM AST on RAP1 protein expressions and the digital results. qPCR was performed for 40 cycles. For qPCR, each RNA sample was subjected to three technical replicates ( n = 3). Western blot analysis was performed with three biological replicates. ( n = 3). *, ** and *** represent significant differences at p < 0.05, p < 0.01, and p < 0.001 compared with the negative control group, respectively. # and ### represent significant differences at p < 0.05, p < 0.001 compared with the negative control group for 48 h, respectively.
    Trf2 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+trf2/pmc13024513-63-52-54?v=Cell+Signaling+Technology+Inc
    Average 93 stars, based on 1 article reviews
    trf2 antibody - by Bioz Stars, 2026-07
    93/100 stars
      Buy from Supplier

    95
    Novus Biologicals rabbit anti trf2
    Effect of DISS on telomere. ( A ) The changes in telomerase content after treatment with 0, 1, 3, 10 μM DISS or 10 μM RES. ( B ) Relative telomere length of 3T3 cells after treatment with 0, 1, 3, 10 μM DISS or 10 μM AST. ( C , D ) Effects of 1, 3, 10 μM DISS or 10 μM RES on EST1 , EST2 genes at 24 and 48 h. ( E ) Effects of 0, 1, 3, 10 μM DISS or 10 μM AST on <t>TRF2</t> protein expressions and digital results. ( F ) Effects of 0, 1, 3, 10 μM DISS or 10 μM AST on RAP1 protein expressions and the digital results. qPCR was performed for 40 cycles. For qPCR, each RNA sample was subjected to three technical replicates ( n = 3). Western blot analysis was performed with three biological replicates. ( n = 3). *, ** and *** represent significant differences at p < 0.05, p < 0.01, and p < 0.001 compared with the negative control group, respectively. # and ### represent significant differences at p < 0.05, p < 0.001 compared with the negative control group for 48 h, respectively.
    Rabbit Anti Trf2, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+trf2/pm41712379-430-4-5?v=Novus+Biologicals
    Average 95 stars, based on 1 article reviews
    rabbit anti trf2 - by Bioz Stars, 2026-07
    95/100 stars
      Buy from Supplier

    86
    Cell Signaling Technology Inc trf2 d1y5d rabbit mab
    Regulation of BLM-LI and TSE-LI by IL-17A. ( A ) Lung sections of WT mice exposed to saline or BLM for 24–72 h were subjected to IHC staining for IL-17A antigen ( i ). AECs isolated from WT and IL-17A-deficient mice exposed to saline or BLM were analyzed for apoptosis and Sirt1 expression by Western blotting (WB) three days later ( ii ). Lung sections of WT and IL-17A −/− mice exposed to saline or BLM were subjected to Masson’s trichrome staining 21 days later ( iii ). Whole lung homogenates of WT and IL-17A −/− mice exposed to saline or BLM as in were analyzed for total HYP content ( iv ) or for Col-1 and FN by WB 21 days after BLM ( v ). ( B ) WT, p53 −/− and PAI-1 −/− mice were kept in ambient air or exposed to passive TS for 20 weeks. Total lung homogenates of control mice kept in ambient air, TSE WT mice, and p53 −/− or PAI-1 −/− mice were analyzed for IL-17A and IL-17RA protein by WB ( i ). Total RNA from mice kept in ambient air, TSE WT mice, and p53 −/− or PAI-1 −/− mice was analyzed for IL-17A mRNA ( ii ). AECs from TSE WT and IL-17A −/− mice were analyzed for p53, ACp53, cleaved (Cl.) caspase-3/caspase-3 and Sirt1 by WB ( iii ). AECs from lungs of IL-17A −/− mice kept in ambient air or TSE, as well as mice treated with or without CSP7 or CP, were analyzed for telomere length by qPCR ( iv ). AECs from lungs of IL-17A −/− mice treated as in ( B(iv )) were immunoblotted for the listed proteins ( v ). Lung sections of IL-17A −/− mice treated as in ( B ( iv )) were subjected to IHC for telomere binding shelterin complex (TRF1 and <t>TRF2)</t> proteins ( vi ).
    Trf2 D1y5d Rabbit Mab, 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/product/rabbit+trf2/pmc12940268-11-2-7?v=Cell+Signaling+Technology+Inc
    Average 86 stars, based on 1 article reviews
    trf2 d1y5d rabbit mab - by Bioz Stars, 2026-07
    86/100 stars
      Buy from Supplier

    93
    Cell Signaling Technology Inc 13136s
    Regulation of BLM-LI and TSE-LI by IL-17A. ( A ) Lung sections of WT mice exposed to saline or BLM for 24–72 h were subjected to IHC staining for IL-17A antigen ( i ). AECs isolated from WT and IL-17A-deficient mice exposed to saline or BLM were analyzed for apoptosis and Sirt1 expression by Western blotting (WB) three days later ( ii ). Lung sections of WT and IL-17A −/− mice exposed to saline or BLM were subjected to Masson’s trichrome staining 21 days later ( iii ). Whole lung homogenates of WT and IL-17A −/− mice exposed to saline or BLM as in were analyzed for total HYP content ( iv ) or for Col-1 and FN by WB 21 days after BLM ( v ). ( B ) WT, p53 −/− and PAI-1 −/− mice were kept in ambient air or exposed to passive TS for 20 weeks. Total lung homogenates of control mice kept in ambient air, TSE WT mice, and p53 −/− or PAI-1 −/− mice were analyzed for IL-17A and IL-17RA protein by WB ( i ). Total RNA from mice kept in ambient air, TSE WT mice, and p53 −/− or PAI-1 −/− mice was analyzed for IL-17A mRNA ( ii ). AECs from TSE WT and IL-17A −/− mice were analyzed for p53, ACp53, cleaved (Cl.) caspase-3/caspase-3 and Sirt1 by WB ( iii ). AECs from lungs of IL-17A −/− mice kept in ambient air or TSE, as well as mice treated with or without CSP7 or CP, were analyzed for telomere length by qPCR ( iv ). AECs from lungs of IL-17A −/− mice treated as in ( B(iv )) were immunoblotted for the listed proteins ( v ). Lung sections of IL-17A −/− mice treated as in ( B ( iv )) were subjected to IHC for telomere binding shelterin complex (TRF1 and <t>TRF2)</t> proteins ( vi ).
    13136s, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+trf2/pmc12940268-11-9-7?v=Cell+Signaling+Technology+Inc
    Average 93 stars, based on 1 article reviews
    13136s - by Bioz Stars, 2026-07
    93/100 stars
      Buy from Supplier

    93
    Cell Signaling Technology Inc trf2
    (a) SDS-PAGE analysis of purified shelterin variants. Replication reactions performed for 20 min on ‘short’ control or telomeric templates in the presence or absence of shelterin at the indicated concentrations were analysed by native and denaturing alkaline agarose electrophoresis as indicated. Position of the stall is indicated. Note the shorter telomeric length compared with figures 1 and 2. The percentage stalled forks after denaturing alkaline electrophoresis compared with reactions lacking shelterin is shown. Average of three independent experiments. Error bars show S.E.M. (b) Pulse chase analysis with ‘short’ control and telomeric templates in the presence or absence of shelterin. Chase added after 50 s and samples taken at the times indicated after initiation and analysed by native and denaturing alkaline agarose electrophoresis. (c) Products from replication reactions performed for 20 min with ‘long’ templates containing C- or G-rich telomeric DNA as the leading strand template with the shelterin concentrations indicated were analysed as in a. (d) Products from replication reactions performed for 20 min on ‘short’ telomeric templates in the presence or absence of shelterin or shelterin variants as indicated were analysed as in a. (e) Products from replication reactions performed for 20 min on ‘short’ telomeric template with shelterin variants indicated were analysed as in a. Δmyb <t>TRF1/TRF2</t> - shelterin in which both TRF1 and TRF2 are lacking myb domains.
    Trf2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+trf2/bio_rxiv__2025__11__13__688213-393-0-6?v=Cell+Signaling+Technology+Inc
    Average 93 stars, based on 1 article reviews
    trf2 - by Bioz Stars, 2026-07
    93/100 stars
      Buy from Supplier

    93
    Novus Biologicals rabbit trf2
    (a) SDS-PAGE analysis of purified shelterin variants. Replication reactions performed for 20 min on ‘short’ control or telomeric templates in the presence or absence of shelterin at the indicated concentrations were analysed by native and denaturing alkaline agarose electrophoresis as indicated. Position of the stall is indicated. Note the shorter telomeric length compared with figures 1 and 2. The percentage stalled forks after denaturing alkaline electrophoresis compared with reactions lacking shelterin is shown. Average of three independent experiments. Error bars show S.E.M. (b) Pulse chase analysis with ‘short’ control and telomeric templates in the presence or absence of shelterin. Chase added after 50 s and samples taken at the times indicated after initiation and analysed by native and denaturing alkaline agarose electrophoresis. (c) Products from replication reactions performed for 20 min with ‘long’ templates containing C- or G-rich telomeric DNA as the leading strand template with the shelterin concentrations indicated were analysed as in a. (d) Products from replication reactions performed for 20 min on ‘short’ telomeric templates in the presence or absence of shelterin or shelterin variants as indicated were analysed as in a. (e) Products from replication reactions performed for 20 min on ‘short’ telomeric template with shelterin variants indicated were analysed as in a. Δmyb <t>TRF1/TRF2</t> - shelterin in which both TRF1 and TRF2 are lacking myb domains.
    Rabbit Trf2, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+trf2/pmc12221885-217-22-24?v=Novus+Biologicals
    Average 93 stars, based on 1 article reviews
    rabbit trf2 - by Bioz Stars, 2026-07
    93/100 stars
      Buy from Supplier

    93
    Cell Signaling Technology Inc anti trf2
    (a) SDS-PAGE analysis of purified shelterin variants. Replication reactions performed for 20 min on ‘short’ control or telomeric templates in the presence or absence of shelterin at the indicated concentrations were analysed by native and denaturing alkaline agarose electrophoresis as indicated. Position of the stall is indicated. Note the shorter telomeric length compared with figures 1 and 2. The percentage stalled forks after denaturing alkaline electrophoresis compared with reactions lacking shelterin is shown. Average of three independent experiments. Error bars show S.E.M. (b) Pulse chase analysis with ‘short’ control and telomeric templates in the presence or absence of shelterin. Chase added after 50 s and samples taken at the times indicated after initiation and analysed by native and denaturing alkaline agarose electrophoresis. (c) Products from replication reactions performed for 20 min with ‘long’ templates containing C- or G-rich telomeric DNA as the leading strand template with the shelterin concentrations indicated were analysed as in a. (d) Products from replication reactions performed for 20 min on ‘short’ telomeric templates in the presence or absence of shelterin or shelterin variants as indicated were analysed as in a. (e) Products from replication reactions performed for 20 min on ‘short’ telomeric template with shelterin variants indicated were analysed as in a. Δmyb <t>TRF1/TRF2</t> - shelterin in which both TRF1 and TRF2 are lacking myb domains.
    Anti Trf2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+trf2/pm40253806-101-6-18?v=Cell+Signaling+Technology+Inc
    Average 93 stars, based on 1 article reviews
    anti trf2 - by Bioz Stars, 2026-07
    93/100 stars
      Buy from Supplier

    93
    Cell Signaling Technology Inc antibody d1y5d
    (a) SDS-PAGE analysis of purified shelterin variants. Replication reactions performed for 20 min on ‘short’ control or telomeric templates in the presence or absence of shelterin at the indicated concentrations were analysed by native and denaturing alkaline agarose electrophoresis as indicated. Position of the stall is indicated. Note the shorter telomeric length compared with figures 1 and 2. The percentage stalled forks after denaturing alkaline electrophoresis compared with reactions lacking shelterin is shown. Average of three independent experiments. Error bars show S.E.M. (b) Pulse chase analysis with ‘short’ control and telomeric templates in the presence or absence of shelterin. Chase added after 50 s and samples taken at the times indicated after initiation and analysed by native and denaturing alkaline agarose electrophoresis. (c) Products from replication reactions performed for 20 min with ‘long’ templates containing C- or G-rich telomeric DNA as the leading strand template with the shelterin concentrations indicated were analysed as in a. (d) Products from replication reactions performed for 20 min on ‘short’ telomeric templates in the presence or absence of shelterin or shelterin variants as indicated were analysed as in a. (e) Products from replication reactions performed for 20 min on ‘short’ telomeric template with shelterin variants indicated were analysed as in a. Δmyb <t>TRF1/TRF2</t> - shelterin in which both TRF1 and TRF2 are lacking myb domains.
    Antibody D1y5d, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+trf2/pmc12221994-256-16-18?v=Cell+Signaling+Technology+Inc
    Average 93 stars, based on 1 article reviews
    antibody d1y5d - by Bioz Stars, 2026-07
    93/100 stars
      Buy from Supplier

    Image Search Results


    Effect of DISS on telomere. ( A ) The changes in telomerase content after treatment with 0, 1, 3, 10 μM DISS or 10 μM RES. ( B ) Relative telomere length of 3T3 cells after treatment with 0, 1, 3, 10 μM DISS or 10 μM AST. ( C , D ) Effects of 1, 3, 10 μM DISS or 10 μM RES on EST1 , EST2 genes at 24 and 48 h. ( E ) Effects of 0, 1, 3, 10 μM DISS or 10 μM AST on TRF2 protein expressions and digital results. ( F ) Effects of 0, 1, 3, 10 μM DISS or 10 μM AST on RAP1 protein expressions and the digital results. qPCR was performed for 40 cycles. For qPCR, each RNA sample was subjected to three technical replicates ( n = 3). Western blot analysis was performed with three biological replicates. ( n = 3). *, ** and *** represent significant differences at p < 0.05, p < 0.01, and p < 0.001 compared with the negative control group, respectively. # and ### represent significant differences at p < 0.05, p < 0.001 compared with the negative control group for 48 h, respectively.

    Journal: Antioxidants

    Article Title: 3,6′-Disinapoyl Sucrose from Polygalae Radix Exerts Anti-Aging Effects via Modification of Telomeres, SIRT1/p53/p21 Pathway, Oxidative Stress and Autophagy

    doi: 10.3390/antiox15030313

    Figure Lengend Snippet: Effect of DISS on telomere. ( A ) The changes in telomerase content after treatment with 0, 1, 3, 10 μM DISS or 10 μM RES. ( B ) Relative telomere length of 3T3 cells after treatment with 0, 1, 3, 10 μM DISS or 10 μM AST. ( C , D ) Effects of 1, 3, 10 μM DISS or 10 μM RES on EST1 , EST2 genes at 24 and 48 h. ( E ) Effects of 0, 1, 3, 10 μM DISS or 10 μM AST on TRF2 protein expressions and digital results. ( F ) Effects of 0, 1, 3, 10 μM DISS or 10 μM AST on RAP1 protein expressions and the digital results. qPCR was performed for 40 cycles. For qPCR, each RNA sample was subjected to three technical replicates ( n = 3). Western blot analysis was performed with three biological replicates. ( n = 3). *, ** and *** represent significant differences at p < 0.05, p < 0.01, and p < 0.001 compared with the negative control group, respectively. # and ### represent significant differences at p < 0.05, p < 0.001 compared with the negative control group for 48 h, respectively.

    Article Snippet: The first antibodies used in this experiment were as follows: SIRT1 antibody (Cell Signaling Technology, Shanghai, China, #9475, 1:1000), GFP antibody (Wuhan Sanying Biotechnology Co., Ltd., Wuhan, China, 50430-2-AP, 1:1000), p53 antibody (Hangzhou Huaan Biotechnology Co., Ltd., Hangzhou, China, HA722074, 1:1000), p21 antibody (Hangzhou Huaan Biotechnology Co., Ltd., Hangzhou, China, HA722065, 1:1000), TRF2 antibody (Cell Signaling Technology, Shanghai, China, #13136, 1:1000), and RAP1 antibody (Cell Signaling Technology, Shanghai, China, #5433, 1:1000), and β -actin antibody (Hangzhou Daige Biotech Co., Ltd., Hangzhou, China, #db13986, 1:1000).

    Techniques: Western Blot, Negative Control

    Regulation of BLM-LI and TSE-LI by IL-17A. ( A ) Lung sections of WT mice exposed to saline or BLM for 24–72 h were subjected to IHC staining for IL-17A antigen ( i ). AECs isolated from WT and IL-17A-deficient mice exposed to saline or BLM were analyzed for apoptosis and Sirt1 expression by Western blotting (WB) three days later ( ii ). Lung sections of WT and IL-17A −/− mice exposed to saline or BLM were subjected to Masson’s trichrome staining 21 days later ( iii ). Whole lung homogenates of WT and IL-17A −/− mice exposed to saline or BLM as in were analyzed for total HYP content ( iv ) or for Col-1 and FN by WB 21 days after BLM ( v ). ( B ) WT, p53 −/− and PAI-1 −/− mice were kept in ambient air or exposed to passive TS for 20 weeks. Total lung homogenates of control mice kept in ambient air, TSE WT mice, and p53 −/− or PAI-1 −/− mice were analyzed for IL-17A and IL-17RA protein by WB ( i ). Total RNA from mice kept in ambient air, TSE WT mice, and p53 −/− or PAI-1 −/− mice was analyzed for IL-17A mRNA ( ii ). AECs from TSE WT and IL-17A −/− mice were analyzed for p53, ACp53, cleaved (Cl.) caspase-3/caspase-3 and Sirt1 by WB ( iii ). AECs from lungs of IL-17A −/− mice kept in ambient air or TSE, as well as mice treated with or without CSP7 or CP, were analyzed for telomere length by qPCR ( iv ). AECs from lungs of IL-17A −/− mice treated as in ( B(iv )) were immunoblotted for the listed proteins ( v ). Lung sections of IL-17A −/− mice treated as in ( B ( iv )) were subjected to IHC for telomere binding shelterin complex (TRF1 and TRF2) proteins ( vi ).

    Journal: International Journal of Molecular Sciences

    Article Title: Interleukin-17A Orchestrates Lung Injury and Remodeling Through p53 and uPA System Crosstalk

    doi: 10.3390/ijms27041841

    Figure Lengend Snippet: Regulation of BLM-LI and TSE-LI by IL-17A. ( A ) Lung sections of WT mice exposed to saline or BLM for 24–72 h were subjected to IHC staining for IL-17A antigen ( i ). AECs isolated from WT and IL-17A-deficient mice exposed to saline or BLM were analyzed for apoptosis and Sirt1 expression by Western blotting (WB) three days later ( ii ). Lung sections of WT and IL-17A −/− mice exposed to saline or BLM were subjected to Masson’s trichrome staining 21 days later ( iii ). Whole lung homogenates of WT and IL-17A −/− mice exposed to saline or BLM as in were analyzed for total HYP content ( iv ) or for Col-1 and FN by WB 21 days after BLM ( v ). ( B ) WT, p53 −/− and PAI-1 −/− mice were kept in ambient air or exposed to passive TS for 20 weeks. Total lung homogenates of control mice kept in ambient air, TSE WT mice, and p53 −/− or PAI-1 −/− mice were analyzed for IL-17A and IL-17RA protein by WB ( i ). Total RNA from mice kept in ambient air, TSE WT mice, and p53 −/− or PAI-1 −/− mice was analyzed for IL-17A mRNA ( ii ). AECs from TSE WT and IL-17A −/− mice were analyzed for p53, ACp53, cleaved (Cl.) caspase-3/caspase-3 and Sirt1 by WB ( iii ). AECs from lungs of IL-17A −/− mice kept in ambient air or TSE, as well as mice treated with or without CSP7 or CP, were analyzed for telomere length by qPCR ( iv ). AECs from lungs of IL-17A −/− mice treated as in ( B(iv )) were immunoblotted for the listed proteins ( v ). Lung sections of IL-17A −/− mice treated as in ( B ( iv )) were subjected to IHC for telomere binding shelterin complex (TRF1 and TRF2) proteins ( vi ).

    Article Snippet: 12 , TRF2 (D1Y5D) rabbit mAb , CST , 13136S , 1:1000 , 1:500.

    Techniques: Saline, Immunohistochemistry, Isolation, Expressing, Western Blot, Staining, Control, Binding Assay

    (a) SDS-PAGE analysis of purified shelterin variants. Replication reactions performed for 20 min on ‘short’ control or telomeric templates in the presence or absence of shelterin at the indicated concentrations were analysed by native and denaturing alkaline agarose electrophoresis as indicated. Position of the stall is indicated. Note the shorter telomeric length compared with figures 1 and 2. The percentage stalled forks after denaturing alkaline electrophoresis compared with reactions lacking shelterin is shown. Average of three independent experiments. Error bars show S.E.M. (b) Pulse chase analysis with ‘short’ control and telomeric templates in the presence or absence of shelterin. Chase added after 50 s and samples taken at the times indicated after initiation and analysed by native and denaturing alkaline agarose electrophoresis. (c) Products from replication reactions performed for 20 min with ‘long’ templates containing C- or G-rich telomeric DNA as the leading strand template with the shelterin concentrations indicated were analysed as in a. (d) Products from replication reactions performed for 20 min on ‘short’ telomeric templates in the presence or absence of shelterin or shelterin variants as indicated were analysed as in a. (e) Products from replication reactions performed for 20 min on ‘short’ telomeric template with shelterin variants indicated were analysed as in a. Δmyb TRF1/TRF2 - shelterin in which both TRF1 and TRF2 are lacking myb domains.

    Journal: bioRxiv

    Article Title: Inhibition of lagging strand replication by G-rich telomeric DNA and the shelterin subunit POT1

    doi: 10.1101/2025.11.13.688213

    Figure Lengend Snippet: (a) SDS-PAGE analysis of purified shelterin variants. Replication reactions performed for 20 min on ‘short’ control or telomeric templates in the presence or absence of shelterin at the indicated concentrations were analysed by native and denaturing alkaline agarose electrophoresis as indicated. Position of the stall is indicated. Note the shorter telomeric length compared with figures 1 and 2. The percentage stalled forks after denaturing alkaline electrophoresis compared with reactions lacking shelterin is shown. Average of three independent experiments. Error bars show S.E.M. (b) Pulse chase analysis with ‘short’ control and telomeric templates in the presence or absence of shelterin. Chase added after 50 s and samples taken at the times indicated after initiation and analysed by native and denaturing alkaline agarose electrophoresis. (c) Products from replication reactions performed for 20 min with ‘long’ templates containing C- or G-rich telomeric DNA as the leading strand template with the shelterin concentrations indicated were analysed as in a. (d) Products from replication reactions performed for 20 min on ‘short’ telomeric templates in the presence or absence of shelterin or shelterin variants as indicated were analysed as in a. (e) Products from replication reactions performed for 20 min on ‘short’ telomeric template with shelterin variants indicated were analysed as in a. Δmyb TRF1/TRF2 - shelterin in which both TRF1 and TRF2 are lacking myb domains.

    Article Snippet: TRF2 was detected with antibody D1Y5D (Cell Signalling, 13136) at 1:5,000 dilution.

    Techniques: SDS Page, Purification, Control, Electrophoresis, Pulse Chase