TRIM41 Antibody Blocking Peptide

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Background: TRIM41

Tripartite motif containing protein 41 or E3 ubiquitin-protein ligase TRIM41 (human TRIM41 theoretical molecular weight 72 kDa) is a RING finger domain protein which catalyzes the degradation of protein kinase C (PKC). TRIM family members share N-terminal RING finger, one or two B box, and Coiled-Coil domains (CCD). The RING (Really Interesting New Gene) finger domain imparts TRIMs with E3 ubiquitin ligase activity and ability to regulate cell cycle, transcription factor, and signal transducing genes. TRIMs are involved in different cellular processes including cellular differentiation, senescence, stem cell pluripotency, and control of microbial infections (1). TRIM41 plays a role in the regulation of innate immunity to viral infections. Hepatitis B virus (HBV) replication is inhibited by TRIM41 in a process dependent on its E3 ligase activity (2, 3). TRIM41 is also involved in the inhibition of influenza A virus (IAV) by ubiquitinating and targeting the influenza nucleoprotein for proteasome degradation (4).

1. Kimura, T., Mandell, M., & Deretic, V. (2016). Precision autophagy directed by receptor regulators - emerging examples within the TRIM family. Journal of Cell Science.https://doi.org/10.1242/jcs.163758

2. Kong, F., You, H., Kong, D., Zheng, K., & Tang, R. (2019). The interaction of hepatitis B virus with the ubiquitin proteasome system in viral replication and associated pathogenesis. Virology Journal. https://doi.org/10.1186/s12985-019-1183-z

3. van Tol, S., Hage, A., Giraldo, M. I., Bharaj, P., & Rajsbaum, R. (2017). The TRIMendous role of TRIMs in virus-host interactions. Vaccines. https://doi.org/10.3390/vaccines5030023

Additional TRIM41 Products

• All Products for TRIM41
• TRIM41 Lysates
• TRIM41 Primary Antibodies
• TRIM41 Proteins and Enzymes

Product Documents for TRIM41 Antibody Blocking Peptide