|Application ||WB, E|
|Calculated MW||191581 Da|
|Antigen Region||25-57 aa|
|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||This JMJD1B antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 25-57 amino acids from the N-terminal region of human JMJD1B.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||JMJD1B Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|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.|
|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.
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.
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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