CHFR (human, recombinant)

Checkpoint with forkhead and RING finger domains protein (CHFR) is an E3 ubiquitin ligase and mitotic checkpoint protein involved in regulation of the cell cycle.¹ It is composed of an N-terminal forkhead-associated domain, a central RING finger domain responsible for its ubiquitinating activity, and a cysteine-rich C-terminal region, which associates with target proteins and contains a RAR-binding zinc-finger (PBZ) domain.² CHFR is ubiquitously expressed, but its levels vary throughout the cell cycle and in response to certain stimuli.¹ It ubiquitinates proteins, such as polo-like kinase (Plk), to target them for degradation and is recruited to sites of DNA damage by poly(ADP-ribose) polymerase 1 (PARP1), to ubiquitinate proteins, including PARP1. Under microtubule stress, such as that induced by microtubule depolymerizing compounds, CHFR levels increase and mitosis is delayed, but under unstressed conditions, CHFR levels decrease as the G₂/M checkpoint approaches and the cell cycle progresses.^2,1,3 CHFR expression is reduced in a variety of cancers, including non-small cell lung cancer (NSCLC), where its reduced expression is associated with poor prognosis.³ Cayman’s CHFR (human, recombinant) protein can be used for enzyme activity assays and has a calculated molecular weight of 73.4 kDa.

WARNING This product is not for human or veterinary use.

1. Derks, S., Cleven, A.H.G., Melotte, V., et al. Emerging evidence for CHFR as a cancer biomarker: From tumor biology to precision medicine. Cancer Metastasis Rev. 33(1), 161-171 (2014).

2. Privette, L.M., and Petty, E.M. CHFR: A Novel mitotic checkpoint protein and regulator of tumorigenesis. Transl. Oncol. 1(2), 57-64 (2008).

3. Sanbhnani, S., and Yeong, F.M. CHFR: A key checkpoint component implicated in a wide range of cancers. Cell. Mol. Life Sci. 69(10), 1669-1687 (2012).