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Purified Mouse Monoclonal Antibody (Mab)
- SPECIFICATION
- CITATIONS
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- BACKGROUND
Application 
| WB, ICC |
|---|---|
| Primary Accession | Q6NYC1 |
| Reactivity | Human |
| Host | Mouse |
| Clonality | Monoclonal |
| Isotype | IgG1 |
| Calculated MW | 62 KDa |
| Gene ID | 23210 |
|---|---|
| Other Names | Apoptotic cell clearance receptor;Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6;Histone arginine demethylase JMJD6;JmjC domain-containing protein 6;JMJD 6;JMJD6;JMJD6_HUMAN;Jumonji domain containing 6;Jumonji domain-containing protein 6;KIAA0585;Lysyl-hydroxylase JMJD6;Peptide-lysine 5-dioxygenase JMJD6;Phosphatidylserine receptor;Protein PTDSR;PSR;PTDSR 1;PTDSR;PTDSR1. |
| Dilution | WB~~1:1000 ICC~~1:200 |
| Format | Purified mouse monoclonal in buffer containing 0.1M Tris-Glycine (pH 7.4, 150 mM NaCl) with 0.02% sodium azide, 50%,glycerol |
| Storage | Store at -20 °C.Stable for 12 months from date of receipt |
| Name | JMJD6 |
|---|---|
| Synonyms | KIAA0585, PTDSR |
| Function | Dioxygenase that can both act as a histone arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Acts as a regulator of RNA splicing by mediating 5-hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by its ability to bind single strand RNA. Also acts as an arginine demethylase which demethylates histone H3 at 'Arg-2' (H3R2me) and histone H4 at 'Arg-3' (H4R3me), thereby playing a role in histone code. However, histone arginine demethylation may not constitute the primary activity in vivo. Has no histone lysine demethylase activity. Required for differentiation of multiple organs during embryogenesis. Acts as a key regulator of hematopoietic differentiation: required for angiogenic sprouting by regulating the pre-mRNA splicing activity of U2AF2/U2AF65. Seems to be necessary for the regulation of macrophage cytokine responses. |
| Cellular Location | Nucleus, nucleoplasm. Nucleus, nucleolus. Note=Mainly found throughout the nucleoplasm outside of regions containing heterochromatic DNA, with some localization in nucleolus. During mitosis, excluded from the nucleus and reappears in the telophase of the cell cycle |
| Tissue Location | Highly expressed in the heart, skeletal muscle and kidney. Expressed at moderate or low level in brain, placenta, lung, liver, pancreas, spleen, thymus, prostate, testis and ovary Up-regulated in many patients with chronic pancreatitis. Expressed in nursing thymic epithelial cells. |
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Background
Dioxygenase that can both act as a histone arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Acts as a regulator of RNA splicing by mediating 5-hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by its ability to bind single strand RNA. Also acts as an arginine demethylase which demethylates histone H3 at 'Arg-2' (H3R2me) and histone H4 at 'Arg-3' (H4R3me), thereby playing a role in histone code. However, histone arginine demethylation may not constitute the primary activity in vivo. Has no histone lysine demethylase activity. Required for differentiation of multiple organs during embryogenesis. Acts as a key regulator of hematopoietic differentiation: required for angiogenic sprouting by regulating the pre-mRNA splicing activity of U2AF2/U2AF65. Seems to be necessary for the regulation of macrophage cytokine responses.
References
Izawa M.,et al.Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
Nagase T.,et al.DNA Res. 5:31-39(1998).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Zody M.C.,et al.Nature 440:1045-1049(2006).
Mural R.J.,et al.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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