Tripartite Motif Containing 21 (RO52) Human Recombinant
TRIM21 Human Recombinant produced in SF9 is a polypeptide chain having a calculated molecular mass of 52 kDa.
TRIM21 is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Tripartite Motif Containing 21 (RO52) Human Recombinant, Biotinylated
TRIM21 Human Recombinant, Biotin produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 52kDa.
TRIM21 is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Tripartite Motif Containing 28 Human Recombinant
Tripartite Motif Containing 33 Human Recombinant
The Tripartite Motif (TRIM) family is a large group of proteins characterized by a conserved tripartite motif at the N-terminus, which includes a RING finger domain, one or two B-box zinc finger domains, and a coiled-coil region . The TRIM family is divided into two groups based on their C-terminal domains: Group 1 proteins have a variety of C-terminal domains, while Group 2 proteins possess a SPRY domain .
Key Biological Properties: TRIM proteins are involved in various cellular processes, including cell proliferation, differentiation, and apoptosis . They function as E3 ubiquitin ligases, mediating the ubiquitination and subsequent degradation of target proteins .
Expression Patterns and Tissue Distribution: TRIM proteins are ubiquitously expressed across different tissues, with some members showing tissue-specific expression patterns . For example, TRIM72 (MG53) is predominantly expressed in striated muscles .
Primary Biological Functions: TRIM proteins play crucial roles in immune responses and pathogen recognition . They are involved in the regulation of innate immunity by modulating the activity of various signaling pathways .
Role in Immune Responses and Pathogen Recognition: Many TRIM proteins are induced by interferons and are essential for the restriction of viral infections . For instance, TRIM5α is known for its role in recognizing and restricting retroviral infections .
Mechanisms with Other Molecules and Cells: TRIM proteins interact with various cellular components through their conserved domains . The RING domain confers E3 ubiquitin ligase activity, while the B-box and coiled-coil regions mediate protein-protein interactions .
Binding Partners and Downstream Signaling Cascades: TRIM proteins often form complexes with other proteins to regulate downstream signaling pathways . For example, TRIM21 interacts with antibodies and targets them for degradation, thereby modulating immune responses .
Regulatory Mechanisms Controlling Expression and Activity: The expression and activity of TRIM proteins are tightly regulated at multiple levels Transcriptional Regulation: TRIM gene expression is regulated by various transcription factors and signaling pathways Post-Translational Modifications: TRIM proteins undergo post-translational modifications such as ubiquitination, sumoylation, and phosphorylation, which modulate their stability and activity .
Biomedical Research: TRIM proteins are extensively studied for their roles in various diseases, including cancer, neurodegenerative diseases, and viral infections Diagnostic Tools: TRIM proteins can serve as biomarkers for disease diagnosis and prognosis Therapeutic Strategies: Targeting TRIM proteins offers potential therapeutic strategies for treating diseases such as cancer and viral infections .
Role Throughout the Life Cycle: TRIM proteins are involved in various stages of the life cycle, from development to aging . They play critical roles in cell proliferation, differentiation, and apoptosis, which are essential for normal development and tissue homeostasis . In aging and disease, dysregulation of TRIM proteins can contribute to the progression of various pathological conditions .