TRF1 Rabbit Recombinant mAb

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  • WB
规格 价格 库存 购买数量
20ul RMB 447.17 现货
100ul RMB 1500.04 现货
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400-668-6834

info@selleck.cn

 

使用信息

抗体应用 wb,ELISA
稀释比例
WB
1:1000
反应性 Human Mouse
MW (kDa) 50kDa
抗体类型 Rabbit
浓度 1mg/ml
储存液配方 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide.
储存条件
(自收到货起)
Store at –20°C.

Datasheet & SDS

生物描述

特异性 TRF1 Rabbit Recombinant mAb detects endogenous levels of total TRF1.
背景 Telomeres play a central role in determining longevity of a cell. TRF1 is a telomeric specific protein whose role is to maintain the telomere. Mammalian telomeric DNA is coated with a telomere-specific protein complex, referred to as shelterin/telosome, which consists of TRF1, TRF2, TIN2, POT1, TPP1 and hRap1. TRF1 interacts directly with TIN2, which binds to TRF2 and TPP1. The shelterin subunits TRF1 and TRF2 bind in a sequence-specific manner to double-stranded telomeric DNA, providing a vital platform for recruitment of additional shelterin proteins as well as non-shelterin factors crucial for the maintenance of telomere length and structure. Both TRF1 and TRF2 are engaged in multiple roles at telomeres including telomere protection, telomere replication, sister telomere resolution and telomere length maintenance. The abundance of TRF1 and TRF2 at telomeres is crucial for the maintenance of telomere length and structure. Both TRF1 and TRF2 are subject to extensive post-translational modification, which in turn contribute to the regulation of their stability, binding activity and localization. For TRF1, phosphorylation at nine different sites (T122, T149, T273, S274, S296, T344, S367, T371 and S435) by six different kinases has been reported to modulate its binding to telomeric DNA and its stability. These kinases include AKT, ATM, Aurora A, CDK1, CK2 and Plk1. In contrast to TRF1, control of TRF2 by phosphorylation is less well understood. Aside from phosphorylation, TRF1 is also subject to tankyrasedependent poly(ADP-ribosy)lation. Poly(ADP-ribosy)lation of TRF1 removes TRF1 from telomeric DNA, rendering it susceptible to proteasome-mediated degradation.

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