ArtNr |
PTM-644 |
Hersteller |
PTM Biolabs
|
Menge |
100 ul |
Kategorie |
|
Typ |
Antibody Monoclonal |
Format |
Lyophilized powder |
Applikationen |
WB, IP, ICC, IHC-P |
Specific against |
Human (Homo sapiens), Mouse (Murine, Mus musculus), Rat (Rattus norvegicus), Monkey (Cynomolgus, Simian) |
Host |
Mouse |
Isotype |
IgG |
Konjugat/Tag |
Unconjugated |
Citations |
Tong Haojie, et al. Essential roles of histone lysine methyltransferases EZH2 and EHMT1 in male embryo development of Phenacoccus solenopsis. Communications Biology, 2024. https://www.nature.com/articles/s42003-024-06705-5. |
ECLASS 10.1 |
42030590 |
ECLASS 11.0 |
42030590 |
UNSPSC |
12352203 |
Alias |
H3K9me2 |
Versandbedingung |
Raumtemperatur |
Lieferbar |
|
Manufacturer - Type |
Primary Antibodies |
Manufacturer - Applications |
WB, IHC-P, ICC/IF, IP |
Manufacturer - Category |
Histone & Histone Modification Antibodies |
Manufacturer - Targets |
Histone H3 |
Shipping Temperature |
Ambient temperature |
Storage Conditions |
Store at -20°C. Avoid freeze/thaw cycles. |
Molecular Weight |
15 |
Stability |
Stable for 12 months from date of receipt/reconstitution. |
Manufacturer - Research Area |
Epigenetics |
Manufacturer - Reactivity |
Human, Mouse, Rat, Monkey, Pharbitis |
Product description |
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation and novel acylations directly affect the accessibility of chromatin to transcription factors and other epigenetic regulators, altering genome stability, gene transcription, etc. Histone methylation occurs primarily at lysine and arginine residues on the amino terminal of core histones. Methylation of histones can either increase or decrease transcription of genes, depending on which amino acids (Lys or Arg) in the histones are methylated and how many methyl groups are attached (mono-, di-, Trimethylation on Lys, mono-di-symmetric/asymmetric methylation on Arg). Mostly, lysine methylation occurs primarily on histone H3 Lys4, 9, 27, 36, 79 and H4 Lys20, while Arginine methylation occurs primarily on histone H3 Arg2, 8, 17, 26 and H4 Arg3. histone methyltransferases (HMTs) and histone demethylases (HDMs) are major regulating factors. |
Purification Method |
Protein G and immunogen affinity purified |
Formula |
PBS, Glycerol, BSA |
PTM |
Dimethyl |
Modification Site |
Lys9 |
Immunogen |
Dimethylated human histone H3 (Lys9) peptide |
Clonality |
Monoclonal |
Background |
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, phosphorylation and novel acylations directly affect the accessibility of chromatin to transcription factors and other epigenetic regulators, altering genome stability, gene transcription, etc. Histone methylation occurs primarily at lysine and arginine residues on the amino terminal of core histones. Methylation of histones can either increase or decrease transcription of genes, depending on which amino acids (Lys or Arg) in the histones are methylated and how many methyl groups are attached (mono-, di-, Trimethylation on Lys, mono-di-symmetric/asymmetric methylation on Arg). Mostly, lysine methylation occurs primarily on histone H3 Lys4, 9, 27, 36, 79 and H4 Lys20, while Arginine methylation occurs primarily on histone H3 Arg2, 8, 17, 26 and H4 Arg3. Histone methylases (HMTs) and histone demethylases (HDMs) are major regulating factors. |
Cellular Localization |
Nucleus |
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