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Cat. Number

070069138556946

Chemical Name

JMJD2A Polyclonal Antibody

References

Synonyms

Lysine-Specific Demethylase 4A
KDM4A
Jumonji Domain Containing 2A

Formulation

antigen-affinity purified IgG in 500 μl TBS, pH 7.4, containing 50% glycerol, 0.5 mg/ml BSA ,and 0.02% sodium azide

Stability

1 year

Storage

-20°C

Shipping

Wet ice in continental US; may vary elsewhere

Specificity

Human JMJD2A

Background Reading

Kim, J., Daniel, J., Espejo, A., et al. Tudor, MBT and chromo domains gauge the degree of lysine methylation. EMBO Rep 7(4) 397-403 (2006).

Anand, R., and Marmorstein, R. Structure and mechanism of lysine-specific demethylase enzymes. J Biol Chem 282(49) 35425-35429 (2007).

Gray, S.G., Iglesias, A.H., Lizcano, F., et al. Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein. J Biol Chem 280(31) 28507-28518 (2005).

Metzger, E., and Schüle, R. The expanding world of histone lysine demethylases. Nat Struct Mol Biol 14(4) 252-254 (2007).

Marmorstein, R., and Trievel, R.C. Histone modifying enzymes: Structures, mechanisms, and specificities. Biochim Biophys Acta 1789 58-68 (2009).

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Size	Global Purchasing
500 µl

Description

Antigen: human recombinant JMJD2A amino acids 1-350 Human recombinant JMJD2A amino acids 1-350 · Host: rabbit · Application(s): WB · Jumonji Domain Containing 2A (JMJD2A) is a lysine specific demethylase with emerging roles in histone modification or epigenetic remodeling.^1,2,3 This JMJD2A polyclonal antibody was raised against a N-terminal recombinant fragment of JMJD2A. This fragment includes amino acids 1-350 including the JMJN and JMJC domains but not the two LAP/PHD zinc finger or Tudor domains of the 1,064 amino acid protein.^4,5 JMJD2A is detected at 135 kDa by western blotting using a DLD1 cell lysate as a positive control. Also, the expression of JMJD2A varies by tissue, and northern blotting suggests skeletal muscle as a negative control and lung as a positive control tissue.⁵

1 Anand, R., and Marmorstein, R. Structure and mechanism of lysine-specific demethylase enzymes. J Biol Chem 282(49) 35425-35429 (2007).

2 Marmorstein, R., and Trievel, R.C. Histone modifying enzymes: Structures, mechanisms, and specificities. Biochim Biophys Acta 1789 58-68 (2009).

3 Kim, J., Daniel, J., Espejo, A., et al. Tudor, MBT and chromo domains gauge the degree of lysine methylation. EMBO Rep 7(4) 397-403 (2006).

4 Metzger, E., and Schüle, R. The expanding world of histone lysine demethylases. Nat Struct Mol Biol 14(4) 252-254 (2007).

5 Gray, S.G., Iglesias, A.H., Lizcano, F., et al. Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein. J Biol Chem 280(31) 28507-28518 (2005).

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