Lysine (K)-Specific Demethylase 6B (Kdm6b) antibody

Antigen: Lysine (K)-Specific Demethylase 6B (Kdm6b)

Synonyms: JMJD3, KIAA0346, Jmjd3, BC038313, mKIAA0346, RP23-5O23.5, 1700064E03Rik, jmjd3, kdm6b, zC237L4.7, si:ch211-237l4.7

Clonality: Polyclonal

Host: Rabbit

Reactivity: Dog (Canine), Human, Mouse (Murine), Rat (Rattus)

Application: Western Blotting (WB)

Catalog no.: ABIN405298

Additional Information

Alternative name: JMJD3 / KDM6B

Gene ID: JMJD3

Immunogen: The immunogen for anti-JMJD3 antibody: synthetic peptide directed towards the N terminal of human JMJD3

Sequence: HRAVDPPGARAAREAFALGGLSCAGAWSSCPPHPPPRSAW LPGGRCSASI

Cross-Reactivity: Dog (Canine), Human, Mouse (Murine), Rat (Rattus)

Format: Lyophilized

Reconstitution: Add 50 µl of distilled water. Final anti-JMJD3 antibody concentration is 1 mg/ml.

Description: JMJD3 is a histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. It plays a central role in regulation of posterior development, by regulating HOX gene expression. It is involved in inflammatory response by participating in macrophage differentiation in case of inflammation by regulating gene expression and macrophage differentiation.

Characteristics: Antigen Size: 1682 amino acids

Molecular Weight: 181kDa

Application Details

Application Notes: WB Suggested Anti-JMJD3 Antibody Titration: 0.2-1 ug/ml
ELISA Titer: 1:312500
Positive Control: Human Lung.

Purification: Affinity Purified

Buffer: PBS

Storage (Long Term): For longer periods of storage, store at -20°C. Avoid repeat freeze-thaw cycles.

Storage (Short Term): Any unfrozen and/or unused material can be stored at 4°C for short term use (< 1 week), and should not be re-frozen.

Restrictions: For Research Use only

Images

WB Suggested Anti-JMJD3 Antibody Titration: 0.2-1 ug/ml
ELISA Titer: 1:312500
Positive Control: Human Lung

Publications

Product: Hong, Cho, Yu et al.: "Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 104, Issue 47, pp. 18439-44, 2007 (PubMed).