Tripartite motif containing 21 (TRIM21) belongs to the TRIM family of proteins which function as anti-retroviral restriction factors and are E3 ubiquitin-protein ligases.
Synonyms: Anti-RNF81; Anti-RO52; Anti-Ro/SSA; Anti-SSA1
Storage: -20C
Application: All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project (www.proteinatlas.org)and as a result, are supported by the most extensive characterization in the industry. The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Biochem Physiol Actions: Tripartite motif containing 21 (TRIM21) is involved in regulation of IgG functions and has a role in innate immunity. It binds specifically to the Fc region of human IgG isotypes 1, 2 and 4 with a conformation dependent interaction. The minimal binding epitope is the C-terminal B30.2 domain. TRIM21 forms a trimer that competes with protein A for binding to IgG Fc and binds to the consensus CH2/CH3 domain interface in the Fc region, overlapping the binding site of several other proteins, like protein A and protein G. It has been shown that it interacts with interferon regulatory factor 3 (IRF3) upon RNA virus infection. TRIM21 interferes with the interaction between Pin1 (peptidyl-prolyl cis/trans isomerase, NIMA-interacting 1) and IRF3, thus preventing IRF3 ubiquitination and degradation.
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