Description
JMJD2D Antibody | 55-122 | Gentaur UK, US & Europe Distribution
Host: Rabbit
Reactivity: Human
Homology: N/A
Immunogen: This JMJD2D antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 484-516 amino acids from the C-terminal region of human JMJD2D.
Research Area: Other
Tested Application: WB
Application: For WB starting dilution is: 1:1000
Specificiy: N/A
Positive Control 1: N/A
Positive Control 2: N/A
Positive Control 3: N/A
Positive Control 4: N/A
Positive Control 5: N/A
Positive Control 6: N/A
Molecular Weight: 59 kDa
Validation: N/A
Isoform: N/A
Purification: This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis
Clonality: Polyclonal
Clone: N/A
Isotype: Rabbit Ig
Conjugate: Unconjugated
Physical State: Liquid
Buffer: Supplied in PBS with 0.09% (W/V) sodium azide.
Concentration: batch dependent
Storage Condition: Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
Alternate Name: Lysine-specific demethylase 4D, 11411-, JmjC domain-containing histone demethylation protein 3D, Jumonji domain-containing protein 2D, KDM4D, JHDM3D, JMJD2D
User Note: Optimal dilutions for each application to be determined by the researcher.
BACKGROUND: Covalent modification of histones plays critical role in regulating chromatin structure and transcription. While most covalent histone modifications are reversible, only recently has it been established that methyl groups are subject to enzymatic removal from histones. A family of novel JmjC domain-containing histone demethylation (JHDM) enzymes have been identified that perform this specific function. Histone demethylation by JHDM proteins requires cofactors Fe (II) and alpha-ketoglutarate. Family members include JHDM1 (demethylating histone 3 at lysine 36) , and JHDM2A as well as JMJD2CH3K9 (both of which demethylate histone 3 at lysine 9) . Contributions of histone demethylase activity to tumor development, decreases in cell proliferation, and hormone-dependent transcriptional activation have been observed.