Recombinant Proteins
Product List
RNF114 Human
Ring Finger Protein 114 Human Recombinant
RNF114 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
RNF181 Human
Ring Finger Protein 181 Human Recombinant
RNF181 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
RNF34 Human
Ring Finger Protein 34 Human Recombinant
RNF4 Human
Ring Finger Protein 4 Human Recombinant
RNF4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
RNF7 Human
Ring Finger Protein 7 Human Recombinant
RNF7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Introduction
The Ring Finger Protein (RFP) is a type of protein characterized by the presence of a RING (Really Interesting New Gene) finger domain. This domain is a zinc finger type that contains a C3HC4 amino acid motif, which binds two zinc cations . The RING finger domain typically consists of 40 to 60 amino acids and is involved in mediating protein-protein interactions, particularly in the ubiquitination pathway . RFPs are classified based on their structural domains and functions, with many acting as E3 ubiquitin ligases .
Key Biological Properties: RFPs are known for their role in ubiquitination, a process that tags proteins for degradation . They are involved in various cellular processes, including DNA repair, transcriptional regulation, and apoptosis .
Expression Patterns and Tissue Distribution: RFPs are ubiquitously expressed in various tissues, with specific expression patterns depending on the type of RFP. For example, some RFPs are highly expressed in immune cells, while others are found in neuronal tissues .
Primary Biological Functions: The primary function of RFPs is to act as E3 ubiquitin ligases, facilitating the transfer of ubiquitin from E2 enzymes to target proteins . This process is crucial for protein degradation, signal transduction, and regulation of various cellular processes .
Role in Immune Responses and Pathogen Recognition: RFPs play a significant role in the immune system by regulating the degradation of key signaling proteins involved in immune responses. They are also involved in the recognition and response to pathogens, helping to modulate the immune response .
Mechanisms with Other Molecules and Cells: RFPs interact with E2 ubiquitin-conjugating enzymes to facilitate the transfer of ubiquitin to target proteins . They also interact with various binding partners, including other proteins and DNA, to regulate their activity .
Binding Partners and Downstream Signaling Cascades: RFPs bind to specific substrates and E2 enzymes, forming a complex that mediates ubiquitination. This process triggers downstream signaling cascades that regulate various cellular functions, including cell cycle progression, DNA repair, and apoptosis .
Regulatory Mechanisms Controlling Expression and Activity: The expression and activity of RFPs are tightly regulated at multiple levels. Transcriptional regulation involves various transcription factors that bind to the promoter regions of RFP genes . Post-translational modifications, such as phosphorylation and ubiquitination, also play a crucial role in regulating the stability and activity of RFPs .
Biomedical Research: RFPs are extensively studied in biomedical research due to their role in various diseases, including cancer, neurodegenerative disorders, and autoimmune diseases .
Diagnostic Tools: RFPs are used as biomarkers for the diagnosis of certain diseases. For example, specific RFPs are used to detect cancerous cells in tissue samples .
Therapeutic Strategies: Targeting RFPs with small molecules or antibodies is a promising therapeutic strategy for treating diseases associated with dysregulated ubiquitination .
Role Throughout the Life Cycle: RFPs play a crucial role throughout the life cycle, from development to aging and disease. During development, they regulate the degradation of key proteins involved in cell differentiation and growth . In aging, dysregulation of RFPs can lead to the accumulation of damaged proteins, contributing to age-related diseases . In disease, mutations or alterations in RFPs are associated with various pathological conditions, including cancer and neurodegenerative disorders .
