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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).

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Product Description

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

Product Usage Information

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


Storage: Supplied in 20 mM potassium phosphate (pH 7.0), 50 mM NaCl, 0.1 mM EDTA, 1 mg/ml BSA and 5% glycerol. 1% DMSO. Store at –20°C.

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.


Entrez-Gene Id 8648
Swiss-Prot Acc. Q15788


For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.

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SRC-1 Blocking Peptide