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Merck

G6919

Sigma-Aldrich

Anti-G9a Methyltransferase antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Sinónimos:

Anti-BAT8, Anti-G9a/NG36, Anti-NG36

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

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

Gene Information

human ... EHMT2(10919)
mouse ... Ehmt2(110147)

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.

Specificity

The antibody recognizes the two isoforms of G9a methyltransferase (~180 kDa and 160 kDa).

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.

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.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, and 15 mM sodium azide.

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.

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Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

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Visite la Librería de documentos

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)
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)
The Lysine Methyltransferase G9a in Immune Cell Differentiation and Function
Scheer S, et al.
Frontiers in Immunology, 8 (2017)
The Lysine Methyltransferase G9a in Immune Cell Differentiation and Function
Scheer S, et al.
Frontiers in immunology, 8 (2017)

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