mouse anti-trf2 antibody 4a794 (Millipore)
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Mouse Anti Trf2 Antibody 4a794, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti-trf2+antibody/anti+trf2/pm36426578-350-7-10
Average 90 stars, based on 1 article reviews
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Incubation:Article Title: MiR ‐182‐3p targets TRF2 and impairs tumor growth of triple‐negative breast cancer Article Snippet: For immune labeling, cells were incubated with Article Title: The structurally conserved TELR region on shelterin protein TPP1 is essential for telomerase processivity but not recruitment Article Snippet: Immunofluorescence staining and FISH were carried out as described previously ( ) with the following antibodies: rabbit anti-GFP antibody (Novus; NB600-308), mouse anti-TRF1 antibody (GeneTex; GTX70304). Article Title: Recruitment of TRF2 to laser-induced DNA damage sites. Article Snippet: Several lines of evidence suggest that the telomere-associated protein TRF2 plays critical roles in the DNA damage response.. TRF2 is rapidly and transiently phosphorylated by an ATM-dependent pathway in response to DNA damage and this DNA damage-induced phosphoryation is essential for the DNA-PKdependent pathway of DNA double-strand break repair (DSB).. However, the type of DNA damage that induces TRF2 localization to the damage sites, the requirement for DNA damage-induced phosphorylation of TRF2 for its recruitment, as well as the detailed kinetics of TRF2 accumulation at DNA damage sites have not been fully investigated. Article Title: MiR-182-3p targets TRF2 and impairs tumor growth of triple-negative breast cancer. Article Snippet: The telomeric repeat-binding factor 2 (TRF2) is a telomere-capping protein that plays a key role in the maintenance of telomere structure and function.. It is highly expressed in different cancer types, and it contributes to cancer progression.. To date, anti-cancer strategies to target TRF2 remain a challenge. Labeling:Article Title: MiR ‐182‐3p targets TRF2 and impairs tumor growth of triple‐negative breast cancer Article Snippet: For immune labeling, cells were incubated with Article Title: The structurally conserved TELR region on shelterin protein TPP1 is essential for telomerase processivity but not recruitment Article Snippet: Immunofluorescence staining and FISH were carried out as described previously ( ) with the following antibodies: rabbit anti-GFP antibody (Novus; NB600-308), mouse anti-TRF1 antibody (GeneTex; GTX70304). Article Title: Recruitment of TRF2 to laser-induced DNA damage sites. Article Snippet: Several lines of evidence suggest that the telomere-associated protein TRF2 plays critical roles in the DNA damage response.. TRF2 is rapidly and transiently phosphorylated by an ATM-dependent pathway in response to DNA damage and this DNA damage-induced phosphoryation is essential for the DNA-PKdependent pathway of DNA double-strand break repair (DSB).. However, the type of DNA damage that induces TRF2 localization to the damage sites, the requirement for DNA damage-induced phosphorylation of TRF2 for its recruitment, as well as the detailed kinetics of TRF2 accumulation at DNA damage sites have not been fully investigated. Article Title: MiR-182-3p targets TRF2 and impairs tumor growth of triple-negative breast cancer. Article Snippet: The telomeric repeat-binding factor 2 (TRF2) is a telomere-capping protein that plays a key role in the maintenance of telomere structure and function.. It is highly expressed in different cancer types, and it contributes to cancer progression.. To date, anti-cancer strategies to target TRF2 remain a challenge. Immunofluorescence:Article Title: MiR ‐182‐3p targets TRF2 and impairs tumor growth of triple‐negative breast cancer Article Snippet: For immune labeling, cells were incubated with Article Title: The structurally conserved TELR region on shelterin protein TPP1 is essential for telomerase processivity but not recruitment Article Snippet: Immunofluorescence staining and FISH were carried out as described previously ( ) with the following antibodies: rabbit anti-GFP antibody (Novus; NB600-308), mouse anti-TRF1 antibody (GeneTex; GTX70304). Article Title: Recruitment of TRF2 to laser-induced DNA damage sites. Article Snippet: Several lines of evidence suggest that the telomere-associated protein TRF2 plays critical roles in the DNA damage response.. TRF2 is rapidly and transiently phosphorylated by an ATM-dependent pathway in response to DNA damage and this DNA damage-induced phosphoryation is essential for the DNA-PKdependent pathway of DNA double-strand break repair (DSB).. However, the type of DNA damage that induces TRF2 localization to the damage sites, the requirement for DNA damage-induced phosphorylation of TRF2 for its recruitment, as well as the detailed kinetics of TRF2 accumulation at DNA damage sites have not been fully investigated. Article Title: MiR-182-3p targets TRF2 and impairs tumor growth of triple-negative breast cancer. Article Snippet: The telomeric repeat-binding factor 2 (TRF2) is a telomere-capping protein that plays a key role in the maintenance of telomere structure and function.. It is highly expressed in different cancer types, and it contributes to cancer progression.. To date, anti-cancer strategies to target TRF2 remain a challenge. Staining:Article Title: MiR ‐182‐3p targets TRF2 and impairs tumor growth of triple‐negative breast cancer Article Snippet: For immune labeling, cells were incubated with Article Title: The structurally conserved TELR region on shelterin protein TPP1 is essential for telomerase processivity but not recruitment Article Snippet: Immunofluorescence staining and FISH were carried out as described previously ( ) with the following antibodies: rabbit anti-GFP antibody (Novus; NB600-308), mouse anti-TRF1 antibody (GeneTex; GTX70304). Article Title: Recruitment of TRF2 to laser-induced DNA damage sites. Article Snippet: Several lines of evidence suggest that the telomere-associated protein TRF2 plays critical roles in the DNA damage response.. TRF2 is rapidly and transiently phosphorylated by an ATM-dependent pathway in response to DNA damage and this DNA damage-induced phosphoryation is essential for the DNA-PKdependent pathway of DNA double-strand break repair (DSB).. However, the type of DNA damage that induces TRF2 localization to the damage sites, the requirement for DNA damage-induced phosphorylation of TRF2 for its recruitment, as well as the detailed kinetics of TRF2 accumulation at DNA damage sites have not been fully investigated. Article Title: MiR-182-3p targets TRF2 and impairs tumor growth of triple-negative breast cancer. Article Snippet: The telomeric repeat-binding factor 2 (TRF2) is a telomere-capping protein that plays a key role in the maintenance of telomere structure and function.. It is highly expressed in different cancer types, and it contributes to cancer progression.. To date, anti-cancer strategies to target TRF2 remain a challenge. Fluorescence In Situ Hybridization:Article Title: MiR ‐182‐3p targets TRF2 and impairs tumor growth of triple‐negative breast cancer Article Snippet: For immune labeling, cells were incubated with Article Title: The structurally conserved TELR region on shelterin protein TPP1 is essential for telomerase processivity but not recruitment Article Snippet: Immunofluorescence staining and FISH were carried out as described previously ( ) with the following antibodies: rabbit anti-GFP antibody (Novus; NB600-308), mouse anti-TRF1 antibody (GeneTex; GTX70304). Article Title: Recruitment of TRF2 to laser-induced DNA damage sites. Article Snippet: Several lines of evidence suggest that the telomere-associated protein TRF2 plays critical roles in the DNA damage response.. TRF2 is rapidly and transiently phosphorylated by an ATM-dependent pathway in response to DNA damage and this DNA damage-induced phosphoryation is essential for the DNA-PKdependent pathway of DNA double-strand break repair (DSB).. However, the type of DNA damage that induces TRF2 localization to the damage sites, the requirement for DNA damage-induced phosphorylation of TRF2 for its recruitment, as well as the detailed kinetics of TRF2 accumulation at DNA damage sites have not been fully investigated. Article Title: MiR-182-3p targets TRF2 and impairs tumor growth of triple-negative breast cancer. Article Snippet: The telomeric repeat-binding factor 2 (TRF2) is a telomere-capping protein that plays a key role in the maintenance of telomere structure and function.. It is highly expressed in different cancer types, and it contributes to cancer progression.. To date, anti-cancer strategies to target TRF2 remain a challenge. Transfection:Article Title: MiR ‐182‐3p targets TRF2 and impairs tumor growth of triple‐negative breast cancer Article Snippet: For immune labeling, cells were incubated with Article Title: The structurally conserved TELR region on shelterin protein TPP1 is essential for telomerase processivity but not recruitment Article Snippet: Immunofluorescence staining and FISH were carried out as described previously ( ) with the following antibodies: rabbit anti-GFP antibody (Novus; NB600-308), mouse anti-TRF1 antibody (GeneTex; GTX70304). Article Title: Recruitment of TRF2 to laser-induced DNA damage sites. Article Snippet: Several lines of evidence suggest that the telomere-associated protein TRF2 plays critical roles in the DNA damage response.. TRF2 is rapidly and transiently phosphorylated by an ATM-dependent pathway in response to DNA damage and this DNA damage-induced phosphoryation is essential for the DNA-PKdependent pathway of DNA double-strand break repair (DSB).. However, the type of DNA damage that induces TRF2 localization to the damage sites, the requirement for DNA damage-induced phosphorylation of TRF2 for its recruitment, as well as the detailed kinetics of TRF2 accumulation at DNA damage sites have not been fully investigated. Article Title: MiR-182-3p targets TRF2 and impairs tumor growth of triple-negative breast cancer. Article Snippet: The telomeric repeat-binding factor 2 (TRF2) is a telomere-capping protein that plays a key role in the maintenance of telomere structure and function.. It is highly expressed in different cancer types, and it contributes to cancer progression.. To date, anti-cancer strategies to target TRF2 remain a challenge. Expressing:Article Title: MiR ‐182‐3p targets TRF2 and impairs tumor growth of triple‐negative breast cancer Article Snippet: For immune labeling, cells were incubated with Article Title: The structurally conserved TELR region on shelterin protein TPP1 is essential for telomerase processivity but not recruitment Article Snippet: Immunofluorescence staining and FISH were carried out as described previously ( ) with the following antibodies: rabbit anti-GFP antibody (Novus; NB600-308), mouse anti-TRF1 antibody (GeneTex; GTX70304). Article Title: Recruitment of TRF2 to laser-induced DNA damage sites. Article Snippet: Several lines of evidence suggest that the telomere-associated protein TRF2 plays critical roles in the DNA damage response.. TRF2 is rapidly and transiently phosphorylated by an ATM-dependent pathway in response to DNA damage and this DNA damage-induced phosphoryation is essential for the DNA-PKdependent pathway of DNA double-strand break repair (DSB).. However, the type of DNA damage that induces TRF2 localization to the damage sites, the requirement for DNA damage-induced phosphorylation of TRF2 for its recruitment, as well as the detailed kinetics of TRF2 accumulation at DNA damage sites have not been fully investigated. Article Title: MiR-182-3p targets TRF2 and impairs tumor growth of triple-negative breast cancer. Article Snippet: The telomeric repeat-binding factor 2 (TRF2) is a telomere-capping protein that plays a key role in the maintenance of telomere structure and function.. It is highly expressed in different cancer types, and it contributes to cancer progression.. To date, anti-cancer strategies to target TRF2 remain a challenge. Construct:Article Title: MiR ‐182‐3p targets TRF2 and impairs tumor growth of triple‐negative breast cancer Article Snippet: For immune labeling, cells were incubated with Article Title: The structurally conserved TELR region on shelterin protein TPP1 is essential for telomerase processivity but not recruitment Article Snippet: Immunofluorescence staining and FISH were carried out as described previously ( ) with the following antibodies: rabbit anti-GFP antibody (Novus; NB600-308), mouse anti-TRF1 antibody (GeneTex; GTX70304). Article Title: Recruitment of TRF2 to laser-induced DNA damage sites. Article Snippet: Several lines of evidence suggest that the telomere-associated protein TRF2 plays critical roles in the DNA damage response.. TRF2 is rapidly and transiently phosphorylated by an ATM-dependent pathway in response to DNA damage and this DNA damage-induced phosphoryation is essential for the DNA-PKdependent pathway of DNA double-strand break repair (DSB).. However, the type of DNA damage that induces TRF2 localization to the damage sites, the requirement for DNA damage-induced phosphorylation of TRF2 for its recruitment, as well as the detailed kinetics of TRF2 accumulation at DNA damage sites have not been fully investigated. Article Title: MiR-182-3p targets TRF2 and impairs tumor growth of triple-negative breast cancer. Article Snippet: The telomeric repeat-binding factor 2 (TRF2) is a telomere-capping protein that plays a key role in the maintenance of telomere structure and function.. It is highly expressed in different cancer types, and it contributes to cancer progression.. To date, anti-cancer strategies to target TRF2 remain a challenge. Immunostaining:Article Title: MiR ‐182‐3p targets TRF2 and impairs tumor growth of triple‐negative breast cancer Article Snippet: For immune labeling, cells were incubated with Article Title: The structurally conserved TELR region on shelterin protein TPP1 is essential for telomerase processivity but not recruitment Article Snippet: Immunofluorescence staining and FISH were carried out as described previously ( ) with the following antibodies: rabbit anti-GFP antibody (Novus; NB600-308), mouse anti-TRF1 antibody (GeneTex; GTX70304). Article Title: Recruitment of TRF2 to laser-induced DNA damage sites. Article Snippet: Several lines of evidence suggest that the telomere-associated protein TRF2 plays critical roles in the DNA damage response.. TRF2 is rapidly and transiently phosphorylated by an ATM-dependent pathway in response to DNA damage and this DNA damage-induced phosphoryation is essential for the DNA-PKdependent pathway of DNA double-strand break repair (DSB).. However, the type of DNA damage that induces TRF2 localization to the damage sites, the requirement for DNA damage-induced phosphorylation of TRF2 for its recruitment, as well as the detailed kinetics of TRF2 accumulation at DNA damage sites have not been fully investigated. Article Title: MiR-182-3p targets TRF2 and impairs tumor growth of triple-negative breast cancer. Article Snippet: The telomeric repeat-binding factor 2 (TRF2) is a telomere-capping protein that plays a key role in the maintenance of telomere structure and function.. It is highly expressed in different cancer types, and it contributes to cancer progression.. To date, anti-cancer strategies to target TRF2 remain a challenge. Two Tailed Test:Article Title: MiR ‐182‐3p targets TRF2 and impairs tumor growth of triple‐negative breast cancer Article Snippet: For immune labeling, cells were incubated with Article Title: The structurally conserved TELR region on shelterin protein TPP1 is essential for telomerase processivity but not recruitment Article Snippet: Immunofluorescence staining and FISH were carried out as described previously ( ) with the following antibodies: rabbit anti-GFP antibody (Novus; NB600-308), mouse anti-TRF1 antibody (GeneTex; GTX70304). Article Title: Recruitment of TRF2 to laser-induced DNA damage sites. Article Snippet: Several lines of evidence suggest that the telomere-associated protein TRF2 plays critical roles in the DNA damage response.. TRF2 is rapidly and transiently phosphorylated by an ATM-dependent pathway in response to DNA damage and this DNA damage-induced phosphoryation is essential for the DNA-PKdependent pathway of DNA double-strand break repair (DSB).. However, the type of DNA damage that induces TRF2 localization to the damage sites, the requirement for DNA damage-induced phosphorylation of TRF2 for its recruitment, as well as the detailed kinetics of TRF2 accumulation at DNA damage sites have not been fully investigated. Article Title: MiR-182-3p targets TRF2 and impairs tumor growth of triple-negative breast cancer. Article Snippet: The telomeric repeat-binding factor 2 (TRF2) is a telomere-capping protein that plays a key role in the maintenance of telomere structure and function.. It is highly expressed in different cancer types, and it contributes to cancer progression.. To date, anti-cancer strategies to target TRF2 remain a challenge. |

