G9a (also known as HLA-B-associated transcript 8 (BAT8), G9a/NG36, or NG36) was originally characterized as a molecule encoded by a gene mapped in the class III region of the human major histocompatibility complex locus. G9a as well as EuHTM1 (Eu-HMTase) were found to be the components of the multimeric protein complex E2F-6.
The antibody recognizes the two isoforms of G9a methyltransferase (~180 kDa and 160 kDa).
synthetic peptide corresponding to amino acids 1193-1210 of human G9a, conjugated to KLH via an N-terminal added lysine residue. This sequence differs from the mouse sequence by 3 amino acids.
Anti-G9a Methyltransferase antibody produced in rabbit has been used in:
- immunohistochemical analysis (IHC)
In vivo, G9a is essential for early embryonic development and plays a dominant role in H3-K9 methylation of euchromatin. G9a was found to be a critical component of the CtBP and E2F-6 transcriptional repressor complexes. G9a was found to be the enzyme responsible for mono and dimethylation within silent euchromatin.
G9a is a lysine-preferring histone methyltransferase (HMTase) containing a SET domain. It has 10 to 20-fold stronger in vitro HMTase activity towards histone H3-Lys9 (H3-K9) when compared to Suv39H1, another member of the same family of HMTases. It also methylates Lys27 of histone H3. Suv39 h1 methylates only lysine 9. It is capable of mono and dimethylation within silent euchromatin, whereas Suv39h1 trimethylates at pericentric heterochromatin. G9a is an important factor in the early embryonic development and plays a dominant role in H3-K9 methylation of euchromatin in vivo. It also forms a crucial component of the CtBP and E2F-6 transcriptional repressor complexes.
Solution in 0.01 M phosphate buffered saline, pH 7.4, and 15 mM sodium azide.
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