G6919
Anti-G9a Methyltransferase antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
Synonym(s):
Anti-BAT8, Anti-G9a/NG36, Anti-NG36
Product Name
Anti-G9a Methyltransferase antibody produced in rabbit, affinity isolated antibody, buffered aqueous solution
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
species reactivity
human
technique(s)
immunoprecipitation (IP): 1-2 μg using 293-T cell extracts
microarray: suitable
western blot: 1-2 μg/mL using nuclear extracts of 293-T cells
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... EHMT2(10919)
mouse ... Ehmt2(110147)
Application
Anti-G9a Methyltransferase antibody produced in rabbit has been used in:
- immunoblotting
- immunoprecipitation
- immunohistochemical analysis (IHC)
Biochem/physiol Actions
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.
The antibody recognizes the two isoforms of G9a methyltransferase (~180 kDa and 160 kDa).
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
General description
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.
Immunogen
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.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, and 15 mM sodium azide.
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Storage Class
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
常规特殊物品
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G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis
Tachibana M, et al.
Genes, 16(14), 1779-1779 (2002)
Inhibition of the H3K9 methyltransferase G9A attenuates oncogenicity and activates the hypoxia signaling pathway
Ho JC, et al.
PLoS ONE, 12(11), e0188051-e0188051 (2017)
The Lysine Methyltransferase G9a in Immune Cell Differentiation and Function
Scheer S, et al.
Frontiers in Immunology, 8 (2017)
Study of methyl transferase (G9aMT) and methylated histone (H3-K9) expressions in unexplained recurrent spontaneous abortion (URSA) and normal early pregnancy
Fatima N, et al.
Molecular Human Reproduction, 17(11), 693-701 (2011)
Methylation of hypoxia-inducible factor (HIF)-1 alpha by G9a/GLP inhibits HIF-1 transcriptional activity and cell migration
Bao L, et al.
Nucleic Acids Research, 46(13), 6576-6591 (2018)
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