Cell Signaling Technology

Product Pathways - Lymphocyte Signaling

NFAT2 (D15F1) Rabbit mAb #8032

Applications Reactivity Sensitivity MW (kDa) Isotype
W IP H M Endogenous 140 Rabbit IgG

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

Protocols

Specificity / Sensitivity

NFAT2 (D15F1) Rabbit mAb detects endogenous levels of total NFAT2 protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ile932 of human NFAT2 protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from Jurkat and CCRF-CEM cells using NFAT2 (D15F1) Rabbit mAb.

Background

The NFAT (nuclear factor of activated T cells) family of proteins consists of NFAT1 (NFATc2 or NFATp), NFAT2 (NFATc1 or NFATc), NFAT3 (NFATc4), and NFAT4 (NFATc3 or NFATx). All members of this family are transcription factors with a Rel homology domain and regulate gene transcription in concert with AP-1 (Jun/Fos) to orchestrate an effective immune response (1,2). NFAT proteins are predominantly expressed in cells of the immune system, but are also expressed in skeletal muscle, keratinocytes, and adipocytes, regulating cell differentiation programs in these cells (3). In resting cells, NFAT proteins are heavily phosphorylated and localized in the cytoplasm. Increased intracellular calcium concentrations activate the calcium/calmodulin-dependent serine phosphatase calcineurin, which dephosphorylates NFAT proteins, resulting in their subsequent translocation to the nucleus (2). Termination of NFAT signaling occurs upon declining calcium concentrations and phosphorylation of NFAT by kinases such as GSK-3 or CK1 (3,4). Cyclosporin A and FK506 are immunosuppressive drugs that inhibit calcineurin and thus retain NFAT proteins in the cytoplasm (5).

  1. Northrop, J.P. et al. (1993) J. Biol. Chem. 268, 2917-2923.
  2. Hogan, P.G. et al. (2003) Genes Dev. 17, 2205-2232.
  3. Crabtree, G.R. and Olson, E.N. (2002) Cell 109, S67-S79.
  4. Okamura, H. et al. (2004) Mol. Cell. Biol. 24, 4184-4195.
  5. Shaw, K.T. et al. (1995) Proc. Natl. Acad. Sci. USA 92, 11205-11209.

Application References

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

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