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AB202239

Recombinant Human JMJD6 protein

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Recombinant Human JMJD6 protein is a Human Full Length protein, in the 1 to 414 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.

View Alternative Names

KIAA0585, PSR, PTDSR, JMJD6, Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6, Histone arginine demethylase JMJD6, JmjC domain-containing protein 6, Jumonji domain-containing protein 6, Lysyl-hydroxylase JMJD6, Peptide-lysine 5-dioxygenase JMJD6, Phosphatidylserine receptor, Protein PTDSR

1 Images
SDS-PAGE - Recombinant Human JMJD6 protein (AB202239)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human JMJD6 protein (AB202239)

15% SDS-PAGE analysis of ab202239 (3μg).

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q6NYC1

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.4 Constituents: PBS, 30% Glycerol (glycerin, glycerine), 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMGSMNHKSKKRIREAKRSARPELKDSLDWTRHNYYESFSLSPAAVADNVERADALQLSVEEFVERYERPYKPVVLLNAQEGWSAQEKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYIEYMESTRDDSPLYIFDSSYGEHPKRRKLLEDYKVPKFFTDDLFQYAGEKRRPPYRWFVMGPPRSGTGIHIDPLGTSAWNALVQGHKRWCLFPTSTPRELIKVTRDEGGNQQDEAITWFNVIYPRTQLPTWPPEFKPLEILQKPGETVFVPGGWWHVVLNLDTTIAITQNFASSTNFPVVWHKTVRGRPKLSRKWYRILKQEHPELAVLADSVDLQESTGIASDSSSDSSSSSSSSSSDSDSECESGSEGDGTVHRRKKRRTCSMVGNGDTTSQDDCVSKERSSSRIRDTCGGRAHP","proteinLength":"Full Length","predictedMolecularWeight":"50 kDa","actualMolecularWeight":null,"aminoAcidEnd":414,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q6NYC1","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

JMJD6 also known as Jumonji Domain Containing 6 or PSR (Phosphatidylserine Receptor) is a protein with a molecular mass of approximately 47 kDa. It functions mechanically as a 2-oxoglutarate- and Fe(II)-dependent oxygenase. This protein resides in the nucleus and cytoplasm with a higher expression in the thymus kidney heart and testis. JMJD6 gets involved in demethylating histones and splicing factors playing a role in gene regulation.
Biological function summary

JMJD6 influences gene expression and mRNA splicing processes. It participates in histone arginine demethylation affecting chromatin structure and transcriptional activity. JMJD6 is not known to be part of a larger protein complex but interacts with RNA splicing factors and chromatin modifiers. Its demethylase activity can alter the epigenetic landscape which makes it a vital part of cellular response and differentiation processes.

Pathways

JMJD6 is linked to the regulation of gene expression and RNA processing pathways. It modulates the transcriptional networks by its demethylase activity affecting how genes are turned on or off. JMJD6 often associates with nuclear receptors and splicing proteins such as SF3B1 integrating within the larger network of gene expression controllers and RNA splicing machinery. These interactions place JMJD6 at a critical juncture in gene expression regulation and RNA maturation.

JMJD6 has connections with cancer and autoimmune diseases. Its role in gene regulation and splicing implicates it in cancer progression often in link with prostate cancer. Abnormal JMJD6 expression can lead to disrupted gene patterns contributing to tumor growth. Additionally its alteration has associations with autoimmune diseases where its interaction with histone-modifying proteins like HDAC affects the immune response. These relationships highlight JMJD6's involvement in disease states marking it as a target of interest in research for therapeutic interventions.
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Specifications

Form

Liquid

Additional notes

Purified using conventional chromatography techniques.

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General info

Function

Dioxygenase that can both act as a arginine demethylase and a lysyl-hydroxylase (PubMed : 17947579, PubMed : 20684070, PubMed : 21060799, PubMed : 22189873, PubMed : 24498420). Acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Regulates RNA splicing by mediating 5-hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65 (PubMed : 19574390). Hydroxylates its own N-terminus, which is required for homooligomerization (PubMed : 22189873). Plays a role in the regulation of nucleolar liquid-liquid phase separation (LLPS) by post-translationally modifying LIAT1 at its lysine-rich domain which inhibits LIAT1 nucleolar targeting (By similarity). 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 : 24360279, PubMed : 24498420). 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/U2AF65 (By similarity). Seems to be necessary for the regulation of macrophage cytokine responses (PubMed : 15622002).

Sequence similarities

Belongs to the JMJD6 family.

Post-translational modifications

Hydroxylates its own N-terminus; hydroxylation is required for homooligomerization.

Subcellular localisation

Nucleus

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Product protocols

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Target data

Dioxygenase that can both act as a arginine demethylase and a lysyl-hydroxylase (PubMed : 17947579, PubMed : 20684070, PubMed : 21060799, PubMed : 22189873, PubMed : 24498420). Acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Regulates RNA splicing by mediating 5-hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65 (PubMed : 19574390). Hydroxylates its own N-terminus, which is required for homooligomerization (PubMed : 22189873). Plays a role in the regulation of nucleolar liquid-liquid phase separation (LLPS) by post-translationally modifying LIAT1 at its lysine-rich domain which inhibits LIAT1 nucleolar targeting (By similarity). 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 : 24360279, PubMed : 24498420). 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/U2AF65 (By similarity). Seems to be necessary for the regulation of macrophage cytokine responses (PubMed : 15622002).
See full target information JMJD6
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