C57BL/6JCya-Ogaem1/Cya
Common Name:
Oga-KO
Product ID:
S-KO-14786
Background:
C57BL/6JCya
Product Type
Age
Genotype
Sex
Quantity
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Basic Information
Strain Name
Oga-KO
Strain ID
KOCMP-76055-Oga-B6J-VA
Gene Name
Product ID
S-KO-14786
Gene Alias
Hy5; Mgea5; Ncoat
Background
C57BL/6JCya
NCBI ID
Modification
Conventional knockout
Chromosome
19
Phenotype
Document
Application
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Note: When using this mouse strain in a publication, please cite “C57BL/6JCya-Ogaem1/Cya mice (Catalog S-KO-14786) were purchased from Cyagen.”
Strain Description
Ensembl Number
ENSMUST00000026243
NCBI RefSeq
NM_023799.4
Target Region
Exon 2~4
Size of Effective Region
~3.0 kb
Detailed Document
Overview of Gene Research
Oga, short for O-GlcNAcase, is the only human enzyme catalyzing the hydrolysis (deglycosylation) of O-linked β-N-acetylglucosaminylation (O-GlcNAcylation) from numerous protein substrates [1]. O-GlcNAcylation is a post-translational modification regulating diverse cellular processes such as signal transduction, cell cycle, metabolism, and energy homeostasis [3]. Dysregulation of O-GlcNAcylation, which Oga plays a crucial role in maintaining, has been implicated in various diseases including cancer, diabetes, and neurodegeneration [2,3].
In triple-negative breast cancer, adipocyte-derived exosomes promote tumor progression through circCRIM1-dependent OGA activation. OGA negatively regulates FBP1 by decreasing its protein stability, and the levels of OGA and FBP1 are related to immune cell infiltration [6]. In DNA damage repair, OGA is recruited to the sites of DNA damage, mediated by O-GlcNAcylation events. Its C-terminal truncated form with the pseudo HAT domain is required for recruitment and for recognizing and deglycosylating DNA repair factors like NONO and the Ku70/80 complex. Suppression of this deglycosylation impairs non-homologous end joining (NHEJ) [4]. In heart failure research, transgenic mouse models with myocardial overexpression of OGA had lower O-GlcNAcylation and were resistant to pathologic stress induced by pressure overload, with decreased pathologic hypertrophy compared to wild-type controls. This suggests enhanced OGA activity is beneficial against pressure overload-induced pathologic remodeling and heart failure [5].
In conclusion, Oga is essential for maintaining O-GlcNAcylation homeostasis, playing a significant role in processes like DNA damage repair, cancer progression, and heart failure. Studies using transgenic mouse models, including overexpression models related to Oga, have provided valuable insights into its functions in these disease-related biological processes, contributing to our understanding of disease mechanisms and potential therapeutic strategies.
References:
1. Hu, Chia-Wei, Wang, Ao, Fan, Dacheng, Li, Lingjun, Jiang, Jiaoyang. 2024. OGA mutant aberrantly hydrolyzes O-GlcNAc modification from PDLIM7 to modulate p53 and cytoskeleton in promoting cancer cell malignancy. In Proceedings of the National Academy of Sciences of the United States of America, 121, e2320867121. doi:10.1073/pnas.2320867121. https://pubmed.ncbi.nlm.nih.gov/38838015/
2. Lu, Ping, Liu, Yusong, He, Maozhou, Yu, Hongtao, Gao, Haishan. 2023. Cryo-EM structure of human O-GlcNAcylation enzyme pair OGT-OGA complex. In Nature communications, 14, 6952. doi:10.1038/s41467-023-42427-8. https://pubmed.ncbi.nlm.nih.gov/37907462/
3. He, Xue-Fen, Hu, Xiaoli, Wen, Gao-Jing, Wang, Zhiwei, Lin, Wen-Jing. 2023. O-GlcNAcylation in cancer development and immunotherapy. In Cancer letters, 566, 216258. doi:10.1016/j.canlet.2023.216258. https://pubmed.ncbi.nlm.nih.gov/37279852/
4. Cui, Yaqi, Xie, Rong, Zhang, Xuefang, Yu, Xiaochun, Wu, Chen. 2021. OGA is associated with deglycosylation of NONO and the KU complex during DNA damage repair. In Cell death & disease, 12, 622. doi:10.1038/s41419-021-03910-6. https://pubmed.ncbi.nlm.nih.gov/34135314/
5. Umapathi, Priya, Mesubi, Olurotimi O, Banerjee, Partha S, Zachara, Natasha E, Anderson, Mark E. 2021. Excessive O-GlcNAcylation Causes Heart Failure and Sudden Death. In Circulation, 143, 1687-1703. doi:10.1161/CIRCULATIONAHA.120.051911. https://pubmed.ncbi.nlm.nih.gov/33593071/
6. Li, Yuehua, Jiang, Baohong, Zeng, Lijun, Zhu, Hongbo, Wu, Yimou. 2023. Adipocyte-derived exosomes promote the progression of triple-negative breast cancer through circCRIM1-dependent OGA activation. In Environmental research, 239, 117266. doi:10.1016/j.envres.2023.117266. https://pubmed.ncbi.nlm.nih.gov/37775001/
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