Data sheet
| Size | 100ug/vial |
| Storage | At -20C for one year. After reconstitution, at 4C for one month. |
| Form | lyophilized |
| Ig type | rabbit IgG |
| Immunogen/Antigen | A synthetic peptide corresponding to a sequence at the C-terminal |
| Reconstitution | 0.2ml of distilled water will yield a concentration of 500μg/ml. |
More info
Background
HDAC3 (HISTONE DEACETYLASE 3) is a member of the histone deacetylase/acuc/apha family of proteins that is an enzyme that in humans is encoded by the HDAC3 gene. The HDAC3 gene is mapped to 5q31.3. HDAC3 has histone deacetylase activity and represses transcription when tethered to a promoter. It may participate in the regulation of transcription through its binding with the zinc-finger transcription factor YY1. The protein can also down-regulate p53 function and thus modulate cell growth and apoptosis. And this gene is regarded as a potential tumor suppressor gene. HDAC3 has an open reading frame of 428 amino acids and shares 53% amino acid identity with HDAC1 and 52% with HDAC2. The catalytic domain of HDAC4 interacts with HDAC3 via the transcriptional corepressor NCOR2. All experimental conditions leading to the suppression of HDAC4 binding to NCOR2 and to HDAC3 resulted in loss of enzymatic activity associated with HDAC4. HDAC3 recruitment to the genome displays a circadian rhythm in mouse liver.
HDAC3 (HISTONE DEACETYLASE 3) is a member of the histone deacetylase/acuc/apha family of proteins that is an enzyme that in humans is encoded by the HDAC3 gene. The HDAC3 gene is mapped to 5q31.3. HDAC3 has histone deacetylase activity and represses transcription when tethered to a promoter. It may participate in the regulation of transcription through its binding with the zinc-finger transcription factor YY1. The protein can also down-regulate p53 function and thus modulate cell growth and apoptosis. And this gene is regarded as a potential tumor suppressor gene. HDAC3 has an open reading frame of 428 amino acids and shares 53% amino acid identity with HDAC1 and 52% with HDAC2. The catalytic domain of HDAC4 interacts with HDAC3 via the transcriptional corepressor NCOR2. All experimental conditions leading to the suppression of HDAC4 binding to NCOR2 and to HDAC3 resulted in loss of enzymatic activity associated with HDAC4. HDAC3 recruitment to the genome displays a circadian rhythm in mouse liver.