R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
TRIM8 (F3C3T) Rabbit mAb #85434
Filter:
- WB
- IP
Supporting Data
REACTIVITY | H |
SENSITIVITY | Endogenous |
MW (kDa) | 62 |
Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
Application | Dilution |
---|---|
Western Blotting | 1:1000 |
Immunoprecipitation | 1:100 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
TRIM8 (F3C3T) Rabbit mAb recognizes endogenous levels of total TRIM8 protein.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro531 of human TRIM8 protein.
Background
Tripartite motif-containing protein 8 (TRIM8) is a RING E3 ubiquitin ligase and member of the TRIM family (1). It was originally termed glioblastoma-expressed RING-finger protein (GERP), encoded by a gene found on a chromosomal region characterized by frequent loss of heterozygosity in glioblastoma (2). The importance of TRIM8 in cancer and other pathological conditions has been described (reviewed in 3,4). Interestingly, TRIM8 has both suppressive and oncogenic activities in cancer. As a tumor suppressor, TRIM8 has the capacity to act in a positive feedback loop to enhance p53 function. TRIM8 is induced by p53 and leads to p53 stabilization by degrading MDM2 (5). In non-small cell lung cancer, TRIM8 functions as a tumor suppressor by targeting MYOF for degradation (6). Other studies illustrated that TRIM8 plays a role in promoting cell proliferation and invasion. TRIM8 regulates cytokine signaling through multiple mechanisms, including inhibition of SOCS1, a suppressor of cytokine signaling (7,8), potentiating TNF-α signaling, and promoting NF-κB activation by targeting TAK1 for K63-linked ubiquitination (9). TRIM8 also interacts with PIAS3, resulting in enhanced STAT3 signaling (10). In ovarian cancer, TRIM8 promotes proliferation by targeting VDAC2 for ubiquitination and degradation (11). In Ewing's sarcoma, TRIM8 promotes survival by targeting the driver fusion EWS/FLI for degradation (12).
- Reymond, A. et al. (2001) EMBO J 20, 2140-51.
- Vincent, S.R. et al. (2000) Biochem Biophys Res Commun 279, 482-6.
- Bhaduri, U. and Merla, G. (2020) Mol Ther Nucleic Acids 22, 434-444.
- Marzano, F. et al. (2021) Cells 10, 561. doi: 10.3390/cells10030561.
- Caratozzolo, M.F. et al. (2012) Cell Cycle 11, 511-23.
- Wei, C.H. et al. (2025) Cell Death Dis 16, 88.
- Toniato, E. et al. (2002) J Biol Chem 277, 37315-22.
- Yu, C. et al. (2024) Biochem Genet , doi: 10.1007/s10528-024-10865-8.
- Li, Q. et al. (2011) Proc Natl Acad Sci USA 108, 19341-6.
- Okumura, F. et al. (2010) J Cell Sci 123, 2238-45.
- Wu, F. et al. (2024) Cancer Med 13, e7396.
- Seong, B.K.A. et al. (2021) Cancer Cell 39, 1262-1278.e7.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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