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HSF2 Sumoylation Site Antibody Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q03933 |
|---|---|
| Clone Names | 2110406 |
| Gene ID | 3298 |
|---|---|
| Other Names | Heat shock factor protein 2, HSF 2, Heat shock transcription factor 2, HSTF 2, HSF2, HSTF2 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP2502a was selected from the region of a human HSF2 sumoylation site. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | HSF2 |
|---|---|
| Synonyms | HSTF2 |
| Function | DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked. |
| Cellular Location | Cytoplasm. Nucleus. Note=Cytoplasmic during normal growth and moves to the nucleus upon activation |
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Provided below are standard protocols that you may find useful for product applications.
Background
HSF2 is a DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked. The protein is found as a DNA-binding homotrimer in stressed or heat shocked cells, and otherwise found as a homodimer. HSF2 is cytoplasmic during normal growth and moves to the nucleus upon activation. Sumoylation of HSF2 hinders HSF2 DNA-binding activity, without affecting its oligomerization, and is an example of negative regulation of gene expression via sumoylation.
References
He, H., et al., J. Biol. Chem. 278(37):35465-35475 (2003).Nykanen, P., et al., Cell Stress Chaperones 6(4):377-385 (2001).Sarge, K.D., et al., Genes Dev. 5(10):1902-1911 (1991).Schuetz, T.J., et al., Proc. Natl. Acad. Sci. U.S.A. 88(16):6911-6915 (1991).
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