Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
Phospho-RIP2 (Ser176) Antibody detects endogenous levels of RIP2 only when phosphorylated at Ser176. Background bands of unknown origin and higher molecular weight are detected.
Polyclonal antibodies are produced by immunizing animals with a phosphopeptide corresponding to residues surrounding Ser176 of human RIP2. Antibodies are purified by protein A and affinity chromatography.
Receptor Interacting Protein 2 (RIP2) is a serine/threonine kinase with a carboxy-terminal caspase activation and recruitment domain (CARD). Association of RIP2 with the tumor necrosis factor receptor (TNFR) causes activation of NF-κB and induction of apoptosis (1-3). Expression of RIP2 is induced in macrophages upon exposure to bacterial cell wall components, such as LPS. RIP2-deficient mouse models demonstrate that this kinase integrates and transduces signals for both the innate and adaptive immune system (4,5).
Serine 176 is a regulatory autophosphorylation site and can be used to monitor the activation state of RIP2 (6).
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