Recombinant TNAP3 protein (His tag)

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Recombinant Human TNFAIP3 (Tumor Necrosis Factor Alpha-Induced Protein 3) Fragment (residues 2-414) is a high-purity protein engineered to encompass the complete OTU domain (residues 92-263). This fragment serves as an essential tool for investigating the ubiquitin-editing functions of TNFAIP3, including its dual deubiquitinase and ubiquitin ligase activities, in immune and inflammatory signaling pathways.

Tumor Necrosis Factor Alpha-Induced Protein 3 (TNFAIP3), also known as A20, is a critical ubiquitin-editing enzyme with both deubiquitinase (EC 3.4.19.12) and ubiquitin ligase (EC 2.3.2.-) activities. It functions as a key negative regulator of NF-kappa-B signaling in response to cytokines (e.g., TNF-alpha, IL-1β) and pathogen-associated molecular patterns via Toll-like receptors. TNFAIP3 terminates inflammatory responses by deubiquitinating 'Lys-63'-linked polyubiquitin chains on signaling molecules like RIPK1 and TRAF6 while promoting 'Lys-48'-linked polyubiquitination, leading to proteasomal degradation. It also inhibits programmed cell death and modulates T-cell receptor signaling by deubiquitinating MALT1. The protein localizes primarily to the cytoplasm, with cleaved forms (A20p50, A20p37) also exhibiting cytoplasmic presence. Its role in immune homeostasis makes it a significant target for studying autoimmune diseases, chronic inflammation, and cancer.