抗TRF-1 (57-6)抗体 | Anti-TRF-1 (57-6) Antibody

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	Western Blot: TRF-1 Antibody (57-6) [NB110-68281] - Detection of TRF1. 50 ugs of total lysate each lane.
	Flow Cytometry: TRF-1 Antibody (57-6) [NB110-68281] - Intracellular flow cytometric staining of 1 x 10^6 CHO (A) and HEK-293 (B) cells using TRF1 antibody (dark blue). Isotype control shown in orange. An antibody concentration of 1 ug/1x10^6 cells was used.
	Western Blot: TRF-1 Antibody (57-6) [NB110-68281] - Detection of TRF1 in HeLa whole cell extracts.
	Simple Western: TRF-1 Antibody (57-6) [NB110-68281] - Simple Western lane view shows a specific band for TRF1 in 0.5 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.

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Background

TRF1 (telomeric repeat-binding factor 1) is a protein that binds telomeric double-stranded TTAGGG repeat and is implicated in telomere replication, telomere protection, telomere length maintenance, resolution of sister telomeres and mitotic spindle regulation. TRF1 interacts directly with TIN2 in shelterin complex (TRF1, TRF2, TIN2, POT1, TPP1 and hRap1; a complex that coats telomeres for their protection and regulation of telomere length) and it then binds to TRF2/TPP1. While POT1 binds to TPP1, TRF2 interacts and forms a complex with hRap1. Upon ionizing DNA damage, TRF1 gets phosphorylated (ser-219) in ATM-dependent manner. ADP-ribosylation by TNKS1 or TNKS2 diminishes TRF1's telomeric DNA binding ability, whereas, RLIM/RNF12 as well as SCF (SKP1-CUL1-F-box protein) can ubiquinate TRF1 for its degradation. TRF1 is ubiquitously expressed and during the cell cycle, its levels are low in G1/S phases which may increase during G2/M phases. Overexpression of TRF1 promotes telomere shortening whereas loss of TRF1 accumulate telomere fusions and induce telomerase-dependent telomere lengthening, implying that TRF1 negatively regulates telomerase-dependent telomere extension, perhaps by restricting the access of telomerase to the ends of telomeres. TRF1 knockout leads to embroynic lethality and deletion of TRF1 promotes the formation of fragile telomeres.

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