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Catalog: YM0389
Size
Price
Status
Qty.
200μL
$600.00
3 weeks

0

100μL
$350.00
3 weeks

0

50μL
$210.00
3 weeks

0

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Collected

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Main Information
Target

JMJD2A

Host Species

Mouse

Reactivity

Human

Applications

WB, IHC, IF, ELISA

MW

121kD (Calculated)

Conjugate/Modification


Unmodified

Detailed Information
Recommended Dilution Ratio
WB 1:500-1:2000; IHC 1:200-1:1000; IF 1:200-1:1000; ELISA 1:10000; Not yet tested in other applications.
Formulation
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Specificity
JMJD2A Monoclonal Antibody detects endogenous levels of JMJD2A protein.
Purification
Affinity purification
Storage
-15°C to -25°C/1 year(Do not lower than -25°C)
MW(Calculated)
121kD
Modification
Unmodified
Clonality
Monoclonal
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Antigen&Target Information
Immunogen:
Purified recombinant fragment of human JMJD2A expressed in E. Coli.
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Specificity:
JMJD2A Monoclonal Antibody detects endogenous levels of JMJD2A protein.
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Gene Name:
KDM4A
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Protein Name:
Lysine-specific demethylase 4A
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Other Name:
KDM4A ;
JHDM3A ;
JMJD2 ;
JMJD2A ;
KIAA0677 ;
Lysine-specific demethylase 4A ;
JmjC domain-containing histone demethylation protein 3A ;
Jumonji domain-containing protein 2A
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Database Link:
Organism Gene ID SwissProt
Human 9682; O75164;
Mouse Q8BW72;
Background:
This gene is a member of the Jumonji domain 2 (JMJD2) family and encodes a protein containing a JmjN domain, a JmjC domain, a JD2H domain, two TUDOR domains, and two PHD-type zinc fingers. This nuclear protein functions as a trimethylation-specific demethylase, converting specific trimethylated histone residues to the dimethylated form, and as a transcriptional repressor. [provided by RefSeq, Apr 2009],
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Function:
cofactor:Binds 1 Fe(2+) ion per subunit.,Domain:The 2 Tudor domains recognize and bind methylated histone H3 'Lys-4' residue. Double Tudor domain has an interdigitated structure and the unusual fold is required for its ability to bind methylated histone tails. Trimethylated H3 'Lys-4' is bound in a cage of 3 aromatic residues, 2 of which are from the Tudor domain 2, while the binding specificity is determined by side-chain interactions involving residues from the Tudor domain 1. The Tudor domains are able to bind trimethylated histone H3 'Lys-4', trimethylated histone H3 'Lys-9', di- and trimethylated H4 'Lys-20'.,Function:Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively.,similarity:Belongs to the JHDM3 histone demethylase family.,similarity:Contains 1 JmjC domain.,similarity:Contains 1 JmjN domain.,similarity:Contains 2 PHD-type zinc fingers.,similarity:Contains 2 Tudor domains.,subunit:Interacts with histone deacetylase proteins HDAC1, HDAC2 and HDAC3. Interacts with RB and NCOR1. Interacts with HTLV-1 Tax protein.,tissue specificity:Ubiquitous.,
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Cellular Localization:
Nucleus .
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Tissue Expression:
Ubiquitous.
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Catalog: YM0389
Size
Price
Status
Qty.
200μL
$600.00
3 weeks

0

100μL
$350.00
3 weeks

0

50μL
$210.00
3 weeks

0

Add to cart

Collected

Collect

Customized Service

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