C57BL/6JCya-Fbxo31em1/Cya
Common Name:
Fbxo31-KO
Product ID:
S-KO-19122
Background:
C57BL/6JCya
Product Type
Age
Genotype
Sex
Quantity
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Contact for Pricing
Basic Information
Strain Name
Fbxo31-KO
Strain ID
KOCMP-76454-Fbxo31-B6J-VB
Gene Name
Product ID
S-KO-19122
Gene Alias
1110003O08Rik; 2310046N15Rik; Fbx14; Fbxo14
Background
C57BL/6JCya
NCBI ID
Modification
Conventional knockout
Chromosome
8
Phenotype
Document
Application
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Note: When using this mouse strain in a publication, please cite “C57BL/6JCya-Fbxo31em1/Cya mice (Catalog S-KO-19122) were purchased from Cyagen.”
Strain Description
Ensembl Number
ENSMUST00000059018
NCBI RefSeq
NM_133765
Target Region
Exon 7
Size of Effective Region
~0.8 kb
Detailed Document
Overview of Gene Research
Fbxo31, a member of the F-box family that constitutes the SCF complex, plays a crucial role in various biological processes. It is involved in ubiquitination-mediated protein degradation, which is essential for regulating multiple cellular pathways such as cell growth, migration, invasion, and redox biology [1,2,3,4,6,7,8,9]. Genetic models, like gene knockout (KO) and conditional knockout (CKO) mouse models, are valuable tools for studying Fbxo31's functions.
In cancer research, FBXO31 shows diverse roles. In pancreatic cancer, it is upregulated by METTL3, promoting cancer progression via regulating SIRT2 ubiquitination and degradation [1]. In contrast, in cholangiocarcinoma, glioma, ovarian cancer, and prostate cancer, its deficiency or down-regulation is associated with tumor initiation, progression, and poor prognosis. For example, in cholangiocarcinoma, FBXO31 functions as a tumor suppressor, sensitizing cancer stem-like cells to cisplatin by promoting ferroptosis and facilitating the proteasomal degradation of GPX4 [2]. In glioma, it suppresses lipogenesis and tumor progression by promoting ubiquitination and degradation of CD147 [3]. In ovarian cancer, c-Myc represses FBXO31 transcription, while FBXO31 facilitates c-Myc polyubiquitination to inhibit cancer growth [6]. In prostate cancer, loss of FBXO31-mediated degradation of DUSP6 dysregulates ERK and PI3K-AKT signaling, promoting tumorigenesis [9]. In esophageal squamous cell carcinoma, high expression of FBXO31 is related to Taxol chemoresistance [7]. Additionally, in premature ovarian insufficiency, aberrantly high FBXO31 in granulosa cells impairs oocyte quality [5]. In liver fibrosis, FBXO31 upregulation promotes hepatic stellate cell activation and fibrogenesis by enhancing Smad7 ubiquitination [8].
In conclusion, Fbxo31 is a key regulator in multiple biological processes, especially in tumorigenesis and cancer progression. Studies using KO/CKO mouse models have revealed its significance in various disease areas, including different types of cancers, premature ovarian insufficiency, and liver fibrosis. Understanding Fbxo31's functions provides potential therapeutic targets for these diseases.
References:
1. Chen, Kai, Wang, Yue, Dai, Xingna, Wang, Zhiwei, Ma, Jia. 2024. FBXO31 is upregulated by METTL3 to promote pancreatic cancer progression via regulating SIRT2 ubiquitination and degradation. In Cell death & disease, 15, 37. doi:10.1038/s41419-024-06425-y. https://pubmed.ncbi.nlm.nih.gov/38216561/
2. Zhu, Zhiwen, Zheng, Yang, He, Huijuan, Dai, Wei, Huang, Haili. 2022. FBXO31 sensitizes cancer stem cells-like cells to cisplatin by promoting ferroptosis and facilitating proteasomal degradation of GPX4 in cholangiocarcinoma. In Liver international : official journal of the International Association for the Study of the Liver, 42, 2871-2888. doi:10.1111/liv.15462. https://pubmed.ncbi.nlm.nih.gov/36269678/
3. Feng, Yan, Liu, Mingli, Xie, Peng, Dong, Ruifeng, Hao, Zhongfei. 2022. FBXO31 suppresses lipogenesis and tumor progression in glioma by promoting ubiquitination and degradation of CD147. In Prostaglandins & other lipid mediators, 163, 106667. doi:10.1016/j.prostaglandins.2022.106667. https://pubmed.ncbi.nlm.nih.gov/35940557/
4. Zhang, Na, Meng, Yang, Mao, Song, Zhang, Yu, Yuan, Kai. 2025. FBXO31-mediated ubiquitination of OGT maintains O-GlcNAcylation homeostasis to restrain endometrial malignancy. In Nature communications, 16, 1274. doi:10.1038/s41467-025-56633-z. https://pubmed.ncbi.nlm.nih.gov/39894887/
5. Zhao, Feiyan, Yan, Long, Zhao, Xuehan, Wang, Hongmei, Yang, Xiaokui. 2024. Aberrantly High FBXO31 Impairs Oocyte Quality in Premature Ovarian Insufficiency. In Aging and disease, 15, 804-823. doi:10.14336/AD.2023.0809. https://pubmed.ncbi.nlm.nih.gov/37611899/
6. Islam, Sehbanul, Dutta, Parul, Sahay, Osheen, Shetty, Praveenkumar, Santra, Manas Kumar. 2022. Feedback-regulated transcriptional repression of FBXO31 by c-Myc triggers ovarian cancer tumorigenesis. In International journal of cancer, 150, 1512-1524. doi:10.1002/ijc.33854. https://pubmed.ncbi.nlm.nih.gov/34706096/
7. Lv, Liang, Wang, Shu Chao, Mo, Jin You, Xu, Mei Li, Liu, Jia. 2021. Effects and mechanisms of FBXO31 on Taxol chemoresistance in esophageal squamous cell carcinoma. In Biochemical and biophysical research communications, 586, 129-136. doi:10.1016/j.bbrc.2021.11.082. https://pubmed.ncbi.nlm.nih.gov/34839191/
8. He, Huijuan, Dai, Jialiang, Feng, Jialing, Xu, Aizhong, Huang, Haili. 2019. FBXO31 modulates activation of hepatic stellate cells and liver fibrogenesis by promoting ubiquitination of Smad7. In Journal of cellular biochemistry, 121, 3711-3719. doi:10.1002/jcb.29528. https://pubmed.ncbi.nlm.nih.gov/31680332/
9. Duan, Shanshan, Moro, Loredana, Qu, Rui, Arbini, Arnaldo A, Pagano, Michele. . Loss of FBXO31-mediated degradation of DUSP6 dysregulates ERK and PI3K-AKT signaling and promotes prostate tumorigenesis. In Cell reports, 37, 109870. doi:10.1016/j.celrep.2021.109870. https://pubmed.ncbi.nlm.nih.gov/34686346/
Quality Control Standard
Sperm Test
Pre-cryopreservation: Measurement of sperm concentration, determination of sperm viability.
Post-cryopreservation: A vial of cryopreserved sperms is selected for in-vitro fertilization from each batch.
Environmental Standards:SPF
Available Region:Global
Source:Cyagen