Description
Post-translational modifications of proteins play critical roles in the regulation and function of many known biological processes. Proteins can be post-translationally modified in many different ways, and a common post-transcriptional modification of lysine involves acetylation.{17715} The conserved amino-terminal domains of the four core histones (H2A, H2B, H3, and H4) contain lysines that are acetylated by histone acetyltransferases (HATs) and deacetylated by histone deacetylases (HDACs).{17716} Protein post-translational reversible lysine Nε-acetylation and deacetylation have been recognized as an emerging intracellular signaling mechanism that plays critical roles in regulating gene transcription, cell-cycle progession, apoptosis, DNA repair, and cytoskeletal orgnization.{17717} The regulation of protein acetylation status is impaired in the pathologies of cancer and polyglutamine diseases, and HDACs have become promising targets for anti-cancer drugs currently in development.{17718,17719}
Synonyms:
Immunogen: acetylated KLH
Formulation: 400 µl (0.25 mg/ml) of rabbit immunoglobulin in PBS containing 0.01% sodium azide
Isotype:
Applications: WB, IP, ELISA, and IF
Origin: Animal/Rabbit
Stability: 365 days
Application|ELISA||Application|Immunofluorescence||Application|Immunoprecipitation||Application|Western Blot||Product Type|Antibodies|Polyclonal Antibodies||Research Area|Epigenetics, Transcription, & Translation|Erasers|Histone Deacetylation||Research Area|Epigenetics, Transcription, & Translation|Histones/Histone Peptides|Acetylated||Research Area|Epigenetics, Transcription, & Translation|Writers|Histone Acetylation
