JMJD1B Blocking Peptide (N-term)
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q7LBC6 |
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Other Accession | Q6ZPY7 |
Gene ID | 51780 |
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Other Names | Lysine-specific demethylase 3B, 11411-, JmjC domain-containing histone demethylation protein 2B, Jumonji domain-containing protein 1B, Nuclear protein 5qNCA, KDM3B, C5orf7, JHDM2B, JMJD1B, KIAA1082 |
Target/Specificity | The synthetic peptide sequence is selected from aa 40-57 of HUMAN KDM3B |
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 | KDM3B |
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Synonyms | C5orf7, JHDM2B, JMJD1B, KIAA1082 |
Function | Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May have tumor suppressor activity. |
Cellular Location | Nucleus. |
Tissue Location | Ubiquitous. Highly expressed in placenta, skeletal muscle, kidney, heart and liver. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Covalent modification of histones plays critical role in regulating chromatin structure and transcription. While most covalent histone modifications are reversible, only recently has it been established that methyl groups are subject to enzymatic removal from histones. A family of novel JmjC domain-containing histone demethylation (JHDM) enzymes have been identified that perform this specific function. Histone demethylation by JHDM proteins requires cofactors Fe(II) and alpha-ketoglutarate. Family members include JHDM1 (demethylating histone 3 at lysine 36), and JHDM2A as well as JMJD2CH3K9 (both of which demethylate histone 3 at lysine 9). Contributions of histone demethylase activity to tumor development, decreases in cell proliferation, and hormone-dependent transcriptional activation have been observed.
References
Katoh, M., et al., Int. J. Mol. Med. 12(5):817-821 (2003).
Hu, Z., et al., Oncogene 20(47):6946-6954 (2001).
Lai, F., et al., Genomics 71(2):235-245 (2001).
Lai, F., et al., Genomics 70(1):123-130 (2000).
Dias Neto, E., et al., Proc. Natl. Acad. Sci. U.S.A. 97(7):3491-3496 (2000).
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