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48-602MAG
Buffer Detection Kit for Magnetic Beads
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07-1534
Sigma-AldrichAnti-JMJD3 Antibody (CT)
Anti-JMJD3 Antibody (C-terminus) is a Rabbit Polyclonal Antibody for detection of JMJD3 Antibody (C-terminus) also known as JmjC domain-containing protein 3 & has been validated in ICC, ELISA & WB.
More>>Anti-JMJD3 Antibody (C-terminus) is a Rabbit Polyclonal Antibody for detection of JMJD3 Antibody (C-terminus) also known as JmjC domain-containing protein 3 & has been validated in ICC, ELISA & WB. Less<<
Anti-JMJD3 Antibody (CT): SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
JMJD3 (Jumonji domain-containing protein 3) is part of the family of novel JmjC domain-containing histone demethylation (JHDM) enzymes. Histone demethylation by JHDM proteins requires cofactors Fe(II) and alpha-ketoglutarate. JMJD3 specifically demethylates Lys27 on histone H3, demethylating both the trimethylated and dimethylated form. JMJD3 plays a role in the regulation of posterior development by regulating HOX gene expression. It is also involved in the inflammatory response by regulating gene expression and macrophage differentiation
References
Product Information
Format
Purified
HS Code
3002 15 90
Control
HeLa cells, NIH/3T3 cells
Presentation
Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide.
Anti-JMJD3 Antibody (C-terminus) is a Rabbit Polyclonal Antibody for detection of JMJD3 Antibody (C-terminus) also known as JmjC domain-containing protein 3 & has been validated in ICC, ELISA & WB.
Key Applications
Immunocytochemistry
ELISA
Western Blotting
Application Notes
Western Blot Analysis: This antibody is reported by an outside laboratory to be suitable for Western blotting
ELISA: This antibody is reported by an outside laboratory to be suitable for ELISA
Biological Information
Immunogen
This antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide selected from the C-terminal region of murine JMJD3.
Epitope
C-terminus
Concentration
Please refer to the Certificate of Analysis for the lot-specific concentration.
Host
Rabbit
Specificity
Recognizes the C-terminal region of murine JMJD3. Additional non-specific, lower molecular weight bands are detected in some lysates.
FUNCTION: Histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. Demethylates trimethylated and dimethylated H3 'Lys-27'. Plays a central role in regulation of posterior development, by regulating HOX gene expression. Involved in inflammatory response by participating in macrophage differentiation in case of inflammation by regulating gene expression and macrophage differentiation. Ref.5 Ref.6
Cofactor Ascorbate By similarity.
Fe(2+). Ref.5
SUBUNIT STRUCTURE: Interacts with TLE1 By similarity. Component of the MLL4 complex, at least composed of MLL4, ASH2L, RBBP5, WDR5, and JMJD3.
SUBCELLULAR lOCATION: NucleusProbable.
INDUCTION: By 12-O-tetradecanoylphorbol-13-acetate (TPA) in myeloid leukemia cells. Ref.4
SIMILARITY: Belongs to the UTX family.
Contains 1 JmjC domain.
Molecular Weight
~180 kDa
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Immunocytochemisty: Recognizes JMJD3 in NIH 3T3 and A431 cells by cytochemistry.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Stable for 1 year at 2-8°C from date of receipt. Handling Recommendations: Upon receipt, and prior to removing the cap, centrifuge the vial to pellet the solution. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
Inadequate functional β cell mass underlies both type 1 and type 2 diabetes. β Cell growth and regeneration also decrease with age through mechanisms that are not fully understood. Age-dependent loss of enhancer of zeste homolog 2 (EZH2) prevents adult β cell replication through derepression of the gene encoding cyclin-dependent kinase inhibitor 2a (INK4a). We investigated whether replenishing EZH2 could reverse the age-dependent increase of Ink4a transcription. We generated an inducible pancreatic β cell-specific Ezh2 transgenic mouse model and showed that transgene expression of Ezh2 was sufficient to increase β cell replication and regeneration in young adult mice. In mice older than 8 months, induction of Ezh2 was unable to repress Ink4a. Older mice had an enrichment of a trithorax group (TrxG) protein complex at the Ink4a locus. Knockdown of TrxG complex components, in conjunction with expression of Ezh2, resulted in Ink4a repression and increased replication of β cells in aged mice. These results indicate that combined modulation of polycomb group proteins, such as EZH2, along with TrxG proteins to repress Ink4a can rejuvenate the replication capacity of aged β cells. This study provides potential therapeutic targets for expansion of adult β cell mass.
Polycomb eviction as a new distant enhancer function. Vernimmen, D; Lynch, MD; De Gobbi, M; Garrick, D; Sharpe, JA; Sloane-Stanley, JA; Smith, AJ; Higgs, DR Genes & development
25
1583-8
2010
Remote distal enhancers may be located tens or thousands of kilobases away from their promoters. How they control gene expression is still poorly understood. Here, we analyze the influence of a remote enhancer on the balance between repression (Polycomb-PcG) and activation (Trithorax-TrxG) of a developmentally regulated gene associated with a CpG island. We reveal its essential, nonredundant role in clearing the PcG complex and H3K27me3 from the CpG island. In the absence of the enhancer, the H3K27me3 demethylase (JMJD3) is not recruited to the CpG island. We propose a new role of long-range regulatory elements in removing repressive PcG complexes.
