TIFA Human
Description
TIFA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
TRAF-Interacting Protein with Forkhead-Associated Domain (TIFA) is a protein that plays a crucial role in the signaling pathways of the immune system. It is known for its interaction with Tumor Necrosis Factor Receptor-Associated Factors (TRAFs), particularly TRAF6, which is involved in the activation of NF-κB, a transcription factor that regulates the expression of various genes involved in immune and inflammatory responses .
TIFA contains a Forkhead-Associated (FHA) domain, which is a phosphopeptide-binding motif. This domain is essential for its function in signal transduction. The FHA domain allows TIFA to bind to phosphorylated serine or threonine residues on other proteins, facilitating the formation of protein complexes that are necessary for downstream signaling events .
TIFA is involved in several biological processes, including:
- NF-κB Activation: TIFA activates TRAF6, leading to the activation of NF-κB. This activation is crucial for the transcription of genes involved in immune responses .
- DNA Damage Response: TIFA transduces DNA damage-induced activation of NF-κB. It accumulates on damaged chromatin following genotoxic stress and enhances the transcription of NF-κB target genes, such as IL-6 and IL-8 .
- Cell Cycle Regulation: TIFA has been shown to inhibit entry into the S phase of the cell cycle, suggesting a role in cell cycle regulation .
Human recombinant TIFA can be produced using recombinant DNA technology. The gene encoding TIFA is cloned into an expression vector, which is then introduced into a suitable host cell, such as E. coli or mammalian cells. The host cells express the TIFA protein, which can be purified using various chromatographic techniques.
TIFA’s activity is regulated through phosphorylation. Phosphorylation at specific threonine residues is crucial for its function in DNA damage response and NF-κB activation. Additionally, TIFA interacts with TRAF2, an E3 ubiquitin ligase, to mediate the ubiquitination of NF-κB essential modulator (NEMO), further regulating NF-κB signaling .
