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Mouse Anti-JMJD6 Recombinant Antibody (CBFYJ-004) (CBMAB-0006-FY)

This product is mouse antibody that recognizes JMJD6. The antibody CBFYJ-004 can be used for immunoassay techniques such as: WB, IF.
See all JMJD6 antibodies

Summary

Host Animal
Mouse
Specificity
Human, Dog, Mouse, Rat
Clone
CBFYJ-004
Antibody Isotype
IgG1
Application
WB, IF

Basic Information

Specificity
Human, Dog, Mouse, Rat
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
jumonji domain containing 6, arginine demethylase and lysine hydroxylase
Introduction
JMJD6 (Arginine Demethylase And Lysine Hydroxylase) encodes a nuclear protein with a JmjC domain. Diseases associated with JMJD6 include Deep Angioma and Intramuscular Hemangioma. Multiple transcript variants encoding different isoforms have been found for this gene. An important paralog of this gene is JMJD4.
Entrez Gene ID
UniProt ID
Alternative Names
PSR; PTDSR; PTDSR1
Function
Dioxygenase that can both act as a arginine demethylase and a lysyl-hydroxylase (PubMed:24498420, PubMed:17947579, PubMed:20684070, PubMed:21060799, PubMed:22189873).
Acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as U2AF2/AC U2AF65 and LUC7L2. Regulates RNA splicing by mediating 5-hydroxylation of U2AF2/AC U2AF65, affecting the pre-mRNA splicing activity of U2AF2/AC U2AF65 (PubMed:19574390).
Hydroxylates its own N-terminus, which is required for homooligomerization (PubMed:22189873).
In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by its ability to bind single strand RNA (PubMed:20679243, PubMed:29176719).
Also acts as an arginine demethylase which preferentially demethylates asymmetric dimethylation (PubMed:17947579, PubMed:24498420, PubMed:24360279).
Demethylates histone H3 at 'Arg-2' (H3R2me) and histone H4 at 'Arg-3' (H4R3me), including mono-, symmetric di- and asymmetric dimethylated forms, thereby playing a role in histone code (PubMed:17947579, PubMed:24360279).
However, histone arginine demethylation may not constitute the primary activity in vivo (PubMed:17947579, PubMed:21060799, PubMed:22189873).
In collaboration with BRD4, interacts with the positive transcription elongation factor b (P-TEFb) complex in its active form to regulate polymerase II promoter-proximal pause release for transcriptional activation of a large cohort of genes. On distal enhancers, so called anti-pause enhancers, demethylates both histone H4R3me2 and the methyl cap of 7SKsnRNA leading to the dismissal of the 7SKsnRNA:HEXIM1 inhibitor complex. After removal of repressive marks, the complex BRD4:JMJD6 attract and retain the P-TEFb complex on chromatin, leading to its activation, promoter-proximal polymerase II pause release, and transcriptional activation (PubMed:24360279).
Demethylates other arginine methylated-proteins such as ESR1 (PubMed:24498420).
Has no histone lysine demethylase activity (PubMed:21060799).
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/AC U2AF65 (By similarity).
Seems to be necessary for the regulation of macrophage cytokine responses (PubMed:15622002).
Biological Process
Cell surface receptor signaling pathwayIEA:Ensembl
Chromatin organizationIEA:UniProtKB-KW
Erythrocyte developmentIEA:Ensembl
Heart developmentIEA:Ensembl
Histone H3-R2 demethylationManual Assertion Based On ExperimentIDA:BHF-UCL
Histone H4-R3 demethylationManual Assertion Based On ExperimentIDA:UniProtKB
Kidney developmentIEA:Ensembl
Lung developmentIEA:Ensembl
Macrophage activationIEA:Ensembl
mRNA processingIEA:UniProtKB-KW
Oxidative RNA demethylationManual Assertion Based On ExperimentIDA:UniProtKB
Peptidyl-lysine hydroxylation to 5-hydroxy-L-lysineManual Assertion Based On ExperimentIDA:UniProtKB
PhagocytosisManual Assertion Based On ExperimentIBA:GO_Central
Positive regulation of transcription by RNA polymerase IIManual Assertion Based On ExperimentIDA:UniProtKB
Positive regulation of transcription, DNA-templatedManual Assertion Based On ExperimentIMP:UniProtKB
Protein demethylationManual Assertion Based On ExperimentIDA:UniProtKB
Protein homooligomerizationManual Assertion Based On ExperimentIDA:UniProtKB
Recognition of apoptotic cellIEA:Ensembl
Regulation of mRNA splicing, via spliceosomeManual Assertion Based On ExperimentIMP:UniProtKB
Retina development in camera-type eyeIEA:Ensembl
RNA splicingIEA:UniProtKB-KW
Sprouting angiogenesisISS:UniProtKB
T cell differentiation in thymusIEA:Ensembl
Cellular Location
Nucleus, nucleoplasm; Nucleus, nucleolus; Cytoplasm. 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.
PTM
Hydroxylates its own N-terminus; hydroxylation is required for homooligomerization.

Xiao, R. Q., Ran, T., Huang, Q. X., Hu, G. S., Fan, D. M., Yi, J., & Liu, W. (2022). A specific JMJD6 inhibitor potently suppresses multiple types of cancers both in vitro and in vivo. Proceedings of the National Academy of Sciences, 119(34), e2200753119.

Wang, K., Yang, C., Li, H., Liu, X., Zheng, M., Xuan, Z., ... & Wang, H. (2022). Role of the epigenetic modifier JMJD6 in tumor development and regulation of immune response. Frontiers in immunology, 13, 859893.

Paschalis, A., Welti, J., Neeb, A. J., Yuan, W., Figueiredo, I., Pereira, R., ... & de Bono, J. S. (2022). JMJD6 is a druggable oxygenase that regulates AR-V7 expression in prostate cancer. Cancer research, 81(4), 1087-1100.

Cockman, M. E., Sugimoto, Y., Pegg, H. B., Masson, N., Salah, E., Tumber, A., ... & Ratcliffe, P. J. (2022). Widespread hydroxylation of unstructured lysine-rich protein domains by JMJD6. Proceedings of the National Academy of Sciences, 119(32), e2201483119.

Wang, T., Zhang, R., Liu, Y., Fang, Z., Zhang, H., Fan, Y., ... & Xiang, R. (2021). Discovery of a new class of JMJD6 inhibitors and structure–activity relationship study. Bioorganic & Medicinal Chemistry Letters, 44, 128109.

Biswas, A., Mukherjee, G., Kondaiah, P., & Desai, K. V. (2020). Both EZH2 and JMJD6 regulate cell cycle genes in breast cancer. BMC cancer, 20(1), 1-12.

Huo, D., Chen, H., Cheng, Y., Song, X., Zhang, K., Li, M. J., & Xuan, C. (2020). JMJD6 modulates DNA damage response through downregulating H4K16ac independently of its enzymatic activity. Cell Death & Differentiation, 27(3), 1052-1066.

Wong, M., Sun, Y., Xi, Z., Milazzo, G., Poulos, R. C., Bartenhagen, C., ... & Liu, T. (2019). JMJD6 is a tumorigenic factor and therapeutic target in neuroblastoma. Nature Communications, 10(1), 3319.

Wan, J., Liu, H., Yang, L., Ma, L., Liu, J., & Ming, L. (2019). JMJD6 promotes hepatocellular carcinoma carcinogenesis by targeting CDK4. International Journal of Cancer, 144(10), 2489-2500.

Ran, T., Xiao, R., Huang, Q., Yuan, H., Lu, T., & Liu, W. (2019). In silico discovery of JMJD6 inhibitors for cancer treatment. ACS Medicinal Chemistry Letters, 10(12), 1609-1613.

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For research use only. Not intended for any clinical use.

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