FADD(Phospho Ser194) Polyclonal Antibody

The protein encoded by this gene is an adaptor molecule that interacts with various cell surface receptors and mediates cell apoptotic signals. Through its C-terminal death domain, this protein can be recruited by TNFRSF6/Fas-receptor, tumor necrosis factor receptor, TNFRSF25, and TNFSF10/TRAIL-receptor, and thus it participates in the death signaling initiated by these receptors. Interaction of this protein with the receptors unmasks the N-terminal effector domain of this protein, which allows it to recruit caspase-8, and thereby activate the cysteine protease cascade. Knockout studies in mice also suggest the importance of this protein in early T cell development.

The FADD(Phospho Ser194) Polyclonal Antibody is a highly specific and sensitive tool designed for the detection and quantification of FADD protein phosphorylated at Ser194. This antibody is produced using advanced polyclonal antibody technology, ensuring high affinity and specificity towards the target protein.

The FADD protein plays a crucial role in the regulation of apoptosis, making it an important target for research in various fields, including cancer biology and immunology. The phosphorylation of FADD at Ser194 has been implicated in the modulation of its function and signaling pathways.

This polyclonal antibody has been rigorously validated for its performance in various applications, including Western blotting, immunoprecipitation, and immunofluorescence. It exhibits excellent sensitivity and specificity, enabling accurate and reliable detection of phosphorylated FADD protein.

The FADD(Phospho Ser194) Polyclonal Antibody is supplied as a liquid formulation, allowing for easy handling and storage. It is provided in a convenient size, ensuring cost-effectiveness and minimizing waste.

With its exceptional performance and reliability, the FADD(Phospho Ser194) Polyclonal Antibody is an indispensable tool for researchers aiming to investigate the role of FADD phosphorylation in cellular processes and disease mechanisms.