Cell Signaling Technology

Product Pathways - NF-kB Signaling

Phospho-RIP2 (Ser176) Antibody #4364

Applications Reactivity Sensitivity MW (kDa) Source
W IP H Endogenous 61 Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

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.

Source / Purification

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.

Western Blotting

Western Blotting

Western blot analysis of extracts from PMA differentiated THP-1 cell lysates untreated or treated with LPS, using Phospho-RIP2 (Ser176) Antibody.

IP

IP

Western blot analysis of extracts and immunoprecipitates from PMA differentiated, LPS induced (10 minutes) THP-1 cell lysates (lane 1). Phospho-RIP2 (Ser176) was immunoprecipitated with Phospho-RIP2 (Ser176) Antibody (lane 2), and specificity was confirmed by immunprecipitation with rabbit IgG (lane 3). Immunoblot was performed using Phospho-RIP2 (Ser176) Antibody.

Background

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).

  1. Inohara, N. et al. (1998) J. Biol. Chem. 273, 12296-12300.
  2. McCarthy, J.V. et al. (1998) J. Biol. Chem. 273, 16968-16975.
  3. Thome, M. et al. (1998) Curr. Biol. 8, 885-888.
  4. Chin, A.I. et al. (2002) Nature 416, 190-194.
  5. Kobayashi, K. et al. (2002) Nature 416, 194-199.
  6. Dorsch, M. et al. (2006) Cell. Signal. 18, 2223-2229.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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