Cell Signaling Technology

Product Pathways - Nuclear Receptor Signaling

SRC-1 Blocking Peptide #1433

Description

This peptide is used to block SRC-1 (128E7) Rabbit mAb #2191 reactivity in immunohistochemistry protocols.

Quality Control

The quality of the peptide was evaluated by reversed-phase HPLC and by mass spectrometry. The peptide blocks SRC-1 (128E7) Rabbit mAb #2191 by immunohistochemistry.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embeded human breast carcinoma using SRC-1 (128E7) Rabbit mAb #2191 in the presence of control peptide (left) or SRC-1 Blocking Peptide (right).

Applications

Use as a blocking reagent to evaluate the specificity of antibody reactivity in immunohistochemistry protocols.

Directions for Use

For immunohistochemistry, add twice the volume of peptide as volume of antibody used in 100 µl total volume. Incubate for a minimum of 30 minutes prior to adding the entire volume to the slide. Recommended antibody dilutions can be found on the relevant product data sheet.

Background

There are three members of the steroid receptor co-activator (SRC) family of proteins: SRC-1 (NCoA-1), SRC-2 (TIF2/GRIP1/NCoA-2), and SRC-3 (ACTR/pCIP/RAC3/TRAM-1/AIB1). All SRC family members share significant structural homology and function to stimulate transcription mediated by nuclear hormone receptors and other transcriptional activators such as Stat3, NF-κB, E2F1, and p53 (1-4). Two SRC proteins, SRC-1 and SRC-3, function as histone acetyltransferases (5,6). In addition, all three family members can recruit other histone acetyltransferases (CBP/p300, PCAF) and histone methyltransferases (PRMT1, CARM1) to target promoters and cooperate to enhance expression of many genes (5-8). The SRC proteins play important roles in multiple physiological processes including cell proliferation, cell survival, somatic cell growth, mammary gland development, female reproductive function, and vasoprotection (9). SRC-1 and SRC-3 are conduits for kinase-mediated growth factor signaling to the estrogen receptor and other transcriptional activators. Seven SRC-1 phosphorylation sites and six SRC-3 phosphorylation sites have been identified, which are induced by steroids, cytokines, and growth factors and involve multiple kinase signaling pathways (9-11). Research has shown that all three SRC family members are associated with increased activity of nuclear receptors in breast, prostate, and ovarian carcinomas. According to the literature, SRC-3 is frequently amplified or overexpressed in a number of cancers (12), and SRC-1/PAX3 and SRC-2/MYST3 translocations are found associated with rhabdomyosarcoma and acute myeloid leukemia, respectively (13,14).

  1. Giraud, S. et al. (2002) J. Biol. Chem. 277, 8004-8011.
  2. Na, S.Y. et al. (1998) J. Biol. Chem. 273, 10831-10834.
  3. Louie, M.C. et al. (2004) Mol. Cell Biol. 24, 5157-5171.
  4. Lee, S.K. et al. (1999) Mol. Endocrinol. 13, 1924-1933.
  5. Spencer, T.E. et al. (1997) Nature 389, 194-198.
  6. Chen, H. et al. (1997) Cell 90, 569-580.
  7. Koh, S.S. et al. (2001) J. Biol. Chem. 276, 1089-1098.
  8. Chen, D. et al. (1999) Science 284, 2174-2177.
  9. Wu, R.C. et al. (2004) Mol. Cell 15, 937-949.
  10. Rowan, B.G. et al. (2000) J. Biol. Chem. 275, 4475-4483.
  11. Zhou, H.J. et al. (2005) Cancer Res. 65, 7976-7983.
  12. Torres-Arzayus, M.I. et al. (2004) Cancer Cell 6, 263-274.
  13. Wachtel, M. et al. (2004) Cancer Res. 64, 5539-5545.
  14. Deguchi, K. et al. (2003) Cancer Cell 3, 259-271.

Application References

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Companion Products

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

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