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Mouse Anti-CHFR Recombinant Antibody (CBWJC-2666) (CBMAB-C3756WJ)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBWJC-2666
Antibody Isotype
IgG1, κ
Application
ELISA, IHC-P, IF

Basic Information

Immunogen
Recombinant Chfr of human.
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal Antibody
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
IF(ICC)1:50-1:500
ELISA1:100-1:1,000
IHC-P1:50-1:500

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% sodium azide
Concentration
0.1 mg/ml
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Checkpoint With Forkhead And Ring Finger Domains
Introduction
This gene encodes an E3 ubiquitin-protein ligase required for the maintenance of the antephase checkpoint that regulates cell cycle entry into mitosis and, therefore, may play a key role in cell cycle progression and tumorigenesis. The encoded protein has an N-terminal forkhead-associated domain, a central RING-finger domain, and a cysteine-rich C-terminal region. Alternatively spliced transcript variants that encode different protein isoforms have been described. [provided by RefSeq, Mar 2014]
Entrez Gene ID
Human55743
Mouse231600
Rat288734
Monkey452391
UniProt ID
HumanQ96EP1
MouseQ810L3
RatQ5PQJ8
MonkeyF7GD73
Alternative Names
Checkpoint With Forkhead And Ring Finger Domains; RING-Type E3 Ubiquitin Transferase CHFR; RING Finger Protein 196; RNF196; Checkpoint With Forkhead And Ring Finger Domains, E3 Ubiquitin Protein Ligase; Checkpoint With Forkhead And RING Finger Domains Protein; E3 Ubiquitin-Protein Ligase CHFR; EC 2.3.2.27; RNF116;
Function
E3 ubiquitin-protein ligase that functions in the antephase checkpoint by actively delaying passage into mitosis in response to microtubule poisons. Acts in early prophase before chromosome condensation, when the centrosome move apart from each other along the periphery of the nucleus. Probably involved in signaling the presence of mitotic stress caused by microtubule poisons by mediating the 'Lys-48'-linked ubiquitination of target proteins, leading to their degradation by the proteasome. Promotes the ubiquitination and subsequent degradation of AURKA and PLK1. Probably acts as a tumor suppressor, possibly by mediating the polyubiquitination of HDAC1, leading to its degradation. May also promote the formation of 'Lys-63'-linked polyubiquitin chains and functions with the specific ubiquitin-conjugating UBC13-MMS2 (UBE2N-UBE2V2) heterodimer. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation, but are rather involved in signaling cellular stress.
Biological Process
Cell division Source: UniProtKB-KW
Meiotic spindle checkpoint Source: UniProtKB
Mitotic cell cycle checkpoint Source: UniProtKB
Modification-dependent protein catabolic process Source: UniProtKB
Positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
Positive regulation of protein ubiquitination Source: Ensembl
Protein destabilization Source: Ensembl
Protein polyubiquitination Source: UniProtKB
Protein ubiquitination Source: GO_Central
Ubiquitin-dependent protein catabolic process Source: GO_Central
Cellular Location
PML body
PTM
Poly-ADP-ribosylated. In addition to binding non covalently poly(ADP-ribose) via its PBZ-type zinc finger, the protein is also covalently poly-ADP-ribosylated by PARP1.
Autoubiquitinated; may regulate its cellular level.
Phosphorylated by PKB. Phosphorylation may affect its E3 ligase activity.
More Infomation

Baretti, M., Karunasena, E., Zahurak, M., Walker, R., Zhao, Y., Pisanic 2nd, T. R., ... & Azad, N. S. (2021). A phase 2 trial of gemcitabine and docetaxel in patients with metastatic colorectal adenocarcinoma with methylated checkpoint with forkhead and ring finger domain promoter and/or microsatellite instability phenotype. Clinical and translational science.

Luo, H., Zhou, Z., Huang, S., Ma, M., Zhao, M., Tang, L., ... & Zhang, P. (2021). CHFR regulates chemoresistance in triple-negative breast cancer through destabilizing ZEB1. Cell death & disease, 12(9), 1-11.

Maekawa, H., Ito, T., Orita, H., Kushida, T., Sakurada, M., Sato, K., ... & Brock, M. V. (2020). Analysis of the methylation of CpG islands in the CDO1, TAC1 and CHFR genes in pancreatic ductal cancer. Oncology letters, 19(3), 2197-2204.

Yang, S., He, F., Dai, M., Pan, J., Wang, J., & Ye, B. (2019). CHFR promotes the migration of human gastric cancer cells by inducing epithelial-to-mesenchymal transition in a HDAC1-dependent manner. OncoTargets and therapy, 12, 1075.

Dai, D., Zhou, B., Xu, W., Jin, H., & Wang, X. (2019). CHFR promoter hypermethylation is associated with gastric cancer and plays a protective role in gastric cancer process. Journal of Cancer, 10(4), 949.

Ding, Y., Lian, H. F., & Du, Y. (2018). Clinicopathological significance of CHFR promoter methylation in gastric cancer: a meta-analysis. Oncotarget, 9(11), 10083.

Zhang, D., Xu, X. L., Li, F., Sun, H. C., Cui, Y. Q., Liu, S., & Xu, P. Y. (2017). Upregulation of the checkpoint protein CHFR is associated with tumor suppression in pancreatic cancers. Oncology letters, 14(6), 8042-8050.

Sun, Z., Liu, J., Jing, H., Dong, S. X., & Wu, J. (2017). The diagnostic and prognostic value of CHFR hypermethylation in colorectal cancer, a meta-analysis and literature review. Oncotarget, 8(51), 89142.

Wang, C., Ma, W., Wei, R., Zhang, X., Shen, N., & Shang, L. (2017). Clinicopathological significance of CHFR methylation in non-small cell lung cancer: a systematic review and meta-analysis. Oncotarget, 8(65), 109732.

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For research use only. Not intended for any clinical use.

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