Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
MORF Antibody detects total levels of endogenous MORF protein. The antibody does not cross-react with other related proteins.
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding amino acid 750 of human MORF. Antibodies are purified by protein A and peptide affinity chromatography.
MORF is a histone acetylase displaying significant sequence homology to MOZ, a monocytic leukemia zinc finger protein. Human MORF is composed of 1781 amino acid residues (1,2). Another two MORF isoforms (MORFalpha and MORFbeta) were cloned, which encode 1890-residue and 2073- residue polypeptides, respectively (1). The difference between MORF and its isoforms is that both MORFalpha and MORFbeta contain extra amino acid residue sequences that are inserted between Pro372 and Aps373 of MORF. In addition to its histone deacetylase domain, MORF contains other multiple functional domains, including a transcriptional repression domain at its N-terminus and a potent activation domain at its C-terminus (1). MORF may be an important transcriptional regulator for both activation and inhibition of gene expression.
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