C57BL/6JCya-Tmem106bem1/Cya
Common Name
Tmem106b-KO
Product ID
S-KO-18411
Backgroud
C57BL/6JCya
Strain ID
KOCMP-71900-Tmem106b-B6J-VB
When using this mouse strain in a publication, please cite “Tmem106b-KO Mouse (Catalog S-KO-18411) were purchased from Cyagen.”
Product Type
Age
Genotype
Sex
Quantity
Basic Information
Strain Name
Tmem106b-KO
Strain ID
KOCMP-71900-Tmem106b-B6J-VB
Gene Name
Product ID
S-KO-18411
Gene Alias
2310036D22Rik, 5830455K21Rik, 6430519M21Rik
Background
C57BL/6JCya
NCBI ID
Modification
Conventional knockout
Chromosome
Chr 6
Phenotype
Datasheet
Application
--
Strain Description
Ensembl Number
ENSMUST00000031556
NCBI RefSeq
NM_027992
Target Region
Exon 4~5
Size of Effective Region
~3.2 kb
Overview of Gene Research
TMEM106B, a lysosomal transmembrane protein, is crucial in regulating multiple aspects of lysosomal function [4]. It also plays a role in myelin lipid metabolism by interacting with galactosylceramidase [5]. Mutations in TMEM106B are risk factors for diverse neurodegenerative diseases [1].
Genetic variation in TMEM106B influences the risk and presentation of neurodegenerative diseases, especially frontotemporal dementia (FTD) caused by mutations in the progranulin gene (GRN) [6]. However, full deletion and partial reduction of TMEM106B in mouse and iPSC-derived human cell models of GRN deficiency did not reverse disease-associated phenotypes, suggesting that lowering TMEM106B levels may not be a viable therapeutic strategy for treating FTD-GRN [7].
In addition, TMEM106B has been found to form amyloid filaments in human brains in an age-dependent manner, which are present in various neurodegenerative diseases [3,6,8,9]. It can also serve as an alternative receptor for SARS-CoV-2 entry into angiotensin-converting enzyme 2 (ACE2)-negative cells [2].
In summary, TMEM106B is integral for lysosomal function and myelin lipid metabolism. Its role in neurodegenerative diseases, especially those related to GRN-associated FTD, has been studied using genetic models. The formation of amyloid filaments and its function as a viral entry receptor further highlight its significance in both neurological and infectious disease contexts.
References：
1. Jiao, Hai-Shan, Yuan, Peng, Yu, Jin-Tai. 2023. TMEM106B aggregation in neurodegenerative diseases: linking genetics to function. In Molecular neurodegeneration, 18, 54. doi:10.1186/s13024-023-00644-1. https://pubmed.ncbi.nlm.nih.gov/37563705/
2. Baggen, Jim, Jacquemyn, Maarten, Persoons, Leentje, Cherepanov, Peter, Daelemans, Dirk. 2023. TMEM106B is a receptor mediating ACE2-independent SARS-CoV-2 cell entry. In Cell, 186, 3427-3442.e22. doi:10.1016/j.cell.2023.06.005. https://pubmed.ncbi.nlm.nih.gov/37421949/
3. Schweighauser, Manuel, Arseni, Diana, Bacioglu, Mehtap, Goedert, Michel, Scheres, Sjors H W. 2022. Age-dependent formation of TMEM106B amyloid filaments in human brains. In Nature, 605, 310-314. doi:10.1038/s41586-022-04650-z. https://pubmed.ncbi.nlm.nih.gov/35344985/
4. Zhu, Min, Zhang, Guoxin, Meng, Lanxia, Fang, Xin, Zhang, Zhentao. 2024. Physiological and pathological functions of TMEM106B in neurodegenerative diseases. In Cellular and molecular life sciences : CMLS, 81, 209. doi:10.1007/s00018-024-05241-z. https://pubmed.ncbi.nlm.nih.gov/38710967/
5. Takahashi, Hideyuki, Perez-Canamas, Azucena, Lee, Chris W, Han, Xianlin, Strittmatter, Stephen M. 2024. Lysosomal TMEM106B interacts with galactosylceramidase to regulate myelin lipid metabolism. In Communications biology, 7, 1088. doi:10.1038/s42003-024-06810-5. https://pubmed.ncbi.nlm.nih.gov/39237682/
6. Perneel, Jolien, Neumann, Manuela, Heeman, Bavo, Rademakers, Rosa, Mackenzie, Ian R A. 2022. Accumulation of TMEM106B C-terminal fragments in neurodegenerative disease and aging. In Acta neuropathologica, 145, 285-302. doi:10.1007/s00401-022-02531-3. https://pubmed.ncbi.nlm.nih.gov/36527486/
7. Dominguez, Sara L, Laufer, Benjamin I, Ghosh, Arundhati Sengupta, Meilandt, William J, Easton, Amy. 2023. TMEM106B reduction does not rescue GRN deficiency in iPSC-derived human microglia and mouse models. In iScience, 26, 108362. doi:10.1016/j.isci.2023.108362. https://pubmed.ncbi.nlm.nih.gov/37965143/
8. Bacioglu, Mehtap, Schweighauser, Manuel, Gray, Derrick, Ghetti, Bernardino, Spillantini, Maria Grazia. 2024. Cleaved TMEM106B forms amyloid aggregates in central and peripheral nervous systems. In Acta neuropathologica communications, 12, 99. doi:10.1186/s40478-024-01813-z. https://pubmed.ncbi.nlm.nih.gov/38886865/
9. Chang, Andrew, Xiang, Xinyu, Wang, Jing, Mackenzie, Ian R A, Fitzpatrick, Anthony W P. 2022. Homotypic fibrillization of TMEM106B across diverse neurodegenerative diseases. In Cell, 185, 1346-1355.e15. doi:10.1016/j.cell.2022.02.026. https://pubmed.ncbi.nlm.nih.gov/35247328/
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
Contact Us
Connect with our experts for your custom animal model needs. Please fill out the form below to start a conversation or request a quote.
Cyagen values your privacy. We’d like to keep you informed about our latest offerings and insights. Your preferences:
You may unsubscribe from these communications at any time. See our Privacy Policy for details on opting out and data protection.
By clicking the button below, you consent to allow Cyagen to store and process the personal information submitted in this form to provide you the content requested.