Anti-Histone H3 (tri methyl K9) Antibody [1-6]

HUABIO

Anti-Histone H3 (tri methyl K9) Antibody [1-6]

7

ImmunoFluorescence, Western Blot, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin

WB,IF-Cell,IHC-P

Research Use Only

Monoclonal

1-6

2 mg/ml

Unconjugated

H3C1

H3 clustered histone 1

H3/A, H3C10, H3C11, H3C12, H3C2, H3C3, H3C4, H3C6, H3C7, H3C8, H3FA, HIST1H3A, histone H3.1, H3 histone family, member A, histone 1, H3a, histone H3/a, histone cluster 1 H3 family member a, histone cluster 1, H3a

Mouse

IgG1

Histone H3.1

Eukaryotic histones are basic and water soluble nuclear proteins that form hetero-octameric nucleosome particles by wrapping 146 base pairs of DNA in a left-handed super-helical turn sequentially to form chromosomal fibers. Two molecules of each of the four core histones (H2A, H2B, H3 and H4) form the octamer, which is comprised of two H2A-H2B dimers and two H3-H4 dimers, forming two nearly symmetrical halves by tertiary structure. Histones are subject to posttranslational modification by enzymes primarily on their N-terminal tails, but also in their globular domains. Human Histone H3 is subject to trimethylation at Lys 9, a modification that may be necessary for select DNA transactions or chromatin state transitions. Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription. Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3).

Human, Mouse, Rat

Human,Mouse,Rat

-20°C,2°C to 8°C

41116161