|Other Names||E3 ubiquitin-protein ligase TRIM22, 632-, 50 kDa-stimulated trans-acting factor, RING finger protein 94, Staf-50, Tripartite motif-containing protein 22, TRIM22, RNF94, STAF50|
|Format||Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Interferon-induced antiviral protein involved in cell innate immunity. The antiviral activity could in part be mediated by TRIM22- dependent ubiquitination of viral proteins. Plays a role in restricting the replication of HIV-1, encephalomyocarditis virus (EMCV) and hepatitis B virus (HBV). Acts as a transcriptional repressor of HBV core promoter. May have E3 ubiquitin-protein ligase activity.|
|Cellular Location||Cytoplasm. Nucleus. Nucleus speckle. Nucleus, Cajal body Note=Localizes predominantly to the nucleus, found in cytoplasm to some extent. Forms distinct nuclear bodies that undergo dynamic changes during cell cycle progression. Nuclear bodies start to form in the early G0/G1 phase but become speckle-like in the S-phase and completely dispersed in mitosis. 35% of TRIM22 nuclear bodies overlap or are found adjacent to Cajal bodies|
|Tissue Location||Strongly expressed in peripheral blood leukocytes, spleen, thymus, and ovary. Expressed at basal levels in other tissues|
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Provided below are standard protocols that you may find useful for product applications.
The protein encoded by this gene is a member of thetripartite motif (TRIM) family. The TRIM motif includes threezinc-binding domains, a RING, a B-box type 1 and a B-box type 2,and a coiled-coil region. This protein localizes to the cytoplasmand its expression is induced by interferon. The proteindown-regulates transcription from the HIV-1 LTR promoter region,suggesting that function of this protein may be to mediateinterferon's antiviral effects.
Kajaste-Rudnitski, A., et al. Amino Acids 39(1):1-9(2010)Petersson, J., et al. Exp. Cell Res. 316(4):568-579(2010)Ovsyannikova, I.G., et al. Hum. Genet. 127(2):207-221(2010)Ovsyannikova, I.G., et al. J. Infect. Dis. 201(2):207-213(2010)Gao, B., et al. Hepatology 50(2):424-433(2009)
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