SET7/9 Protein Crystal(CBCRY57)
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| Product Summary | |
|---|---|
| Name | SET7/9 Protein Crystal |
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| Cat No. | CBCRY57 |
| Fragment | Residues 70-366 |
| Protein Description | SET Domain Containing (Lysine Methyltransferase) 7 |
| Background | Histone-lysine N-methyltransferase SETD7 belongs to histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. It plays a central role in the transcriptional activation of genes such as collagenase or insulin. It can be recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. SETD7 has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation. |
| Protein Classification | Transferase |
| Structure Weight | 33421.14 Da |
| Method | X-Ray Diffraction |
| Resolution | 2.30 Å |
| Ligand Chemical Component | S-ADENOSYLMETHIONINE |
| Reference | Kwon T, Chang JH, Kwak E, Lee CW, Joachimiak A, Kim YC, Lee J, Cho Y. Mechanism of histone lysine methyl transfer revealed by the structure of set7/9-adomet. Embo J. (2003) 22 p.292 |
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