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A20/TNFAIP3: Lysates

A20, also known as TNF-alpha-induced Protein 3 (TNFAIP3) is a 790 amino acid (aa) cytoplasmic protein with a predicted molecular weight of 90 kDa. It was originally described as a protein upregulated by TNF-alpha stimulation. Human A20/TNFAIP3 exhibits 88% aa sequence identity to its mouse ortholog. Structurally, it contains seven zinc finger domains, one of which has Ubiquitin ligase (E3) activity. The N-terminus contains a deubiquitinating enzyme (DUB) domain. As such, A20/TNFAIP3 can be classified as a dual function Ubiquitin editing enzyme. It is known for its ability to modulate inflammatory immune responses by acting as a negative feedback regulator of NF?B signaling. Some putative mechanisms include its ability to modulate upstream components of the NF?B pathway such as RIP1, TRAF2, and TRAF6. Deficiencies in A20/TNFAIP3 have been associated with lymphoid malignancies, and the development of inflammatory and autoimmune disorders.

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A20/TNFAIP3: Lysates

A20, also known as TNF-alpha-induced Protein 3 (TNFAIP3) is a 790 amino acid (aa) cytoplasmic protein with a predicted molecular weight of 90 kDa. It was originally described as a protein upregulated by TNF-alpha stimulation. Human A20/TNFAIP3 exhibits 88% aa sequence identity to its mouse ortholog. Structurally, it contains seven zinc finger domains, one of which has Ubiquitin ligase (E3) activity. The N-terminus contains a deubiquitinating enzyme (DUB) domain. As such, A20/TNFAIP3 can be classified as a dual function Ubiquitin editing enzyme. It is known for its ability to modulate inflammatory immune responses by acting as a negative feedback regulator of NF?B signaling. Some putative mechanisms include its ability to modulate upstream components of the NF?B pathway such as RIP1, TRAF2, and TRAF6. Deficiencies in A20/TNFAIP3 have been associated with lymphoid malignancies, and the development of inflammatory and autoimmune disorders.

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