Technical Data
E2240-20
Elk-1 Control Proteins
150ul
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Technical Data |
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E2240-20 |
Elk-1 Control Proteins |
150ul |
| Molecular Biology | Storage: -20°CShipping: Blue Ice |
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The transcription factor Elk-1 is a component of the ternary complex that binds the serum response element (SRE) and mediates gene activity in response to serum and growth factors (1-3). Elk-1 is phosphorylated by MAP kinase pathways at a cluster of S/T motifs at its carboxy terminus; phosphorylation at these sites, particularly Ser383, is critical for transcriptional activation by Elk-1. Elk-1 appears to be a direct target of activated MAP kinase: (a) biochemical studies indicate that Elk-1 is a good substrate for MAP kinase; (b) the kinetics of Elk-1 phosphorylation and activation correlate with MAP kinase activity; (c) interfering mutants of MAP kinase block Elk-1 activation in vivo. Other studies have shown that Elk-1 (Ser383) is also a target of the stress-activated kinase SAPK/JNK (4,5). Molecular Weight: 40kD nonphosphorylated, 50kD phosphorylated Nonphosphorylated Elk1 fusion protein: Bacterially expressed GST-Elk1 fusion protein serves as a negative control. Supplied in SDS Sample Buffer. Store at -20°C. Phosphorylated Elk1 fusion protein: GST-Elk1 phosphorylated by the Erk2 enzyme serves as a positive control. Supplied in SDS Sample Buffer. Store at -20°C. Directions for Use: As controls, we recommend using 15ul of phosphorylated and nonphosphorylated Elk1 control extracts. Boil sample prior to loading. 150ul wil be sufficient for 10 blots. Western Blots: For controls, we recommend using 15ul of phosphorylated and nonphosphorylated Elk1 control extracts. Boil sample prior to loading. |
Form: Supplied as a liquid in SDS Sample Buffer: 62.5mM Tris-HCl, pH 6.8 at 25°C, 2% w/v SDS, 10% glycerol, 50mM DTT, 0.01% w/v phenol red. Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological. |
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1. Marais, R., Wynne, J. and Treisman, R. (1993) Cell 73:381–393. 2. Kortenjann, M. et al. (1994) Mol. Cell. Biol. 14:4815–4824. 3. Hill, C.S. and Treisman, R. (1995) Cell 80:199–211. 4. Cavigelli, M. et al. (1995) EMBO J. 14:5957–5964. 5. Whitmarsh, A.J. et al. (1995) Science 260:403–406.
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