This histone deacetylase catalyzes the deacetylation of lysine residues on the N-terminal part of core histones (H2A, H2B, H3, and H4), marking them for epigenetic repression. Histone deacetylation plays a crucial role in transcriptional regulation, cell cycle progression, and developmental processes. It operates within large multiprotein complexes, including the NuRD complex, which participates in chromatin remodeling. In the SIN3B complex, it is recruited to transcriptional start sites, suppressing histone acetylation and RNA polymerase II progression, thus regulating transcription. Additionally, it deacetylates non-histone targets such as NR1D2, RELA, SP1, SP3, STAT3, and TSHZ3, modulating their function.
| Product Name | Recombinant Human Histone Deacetylase 1 (HDAC1) Protein (His-SUMO) |
| Accession | Q13547 |
| Purity | Greater than 90% as determined by SDS-PAGE. |
| Host Species | Homo sapiens (Human) |
| Gene | HDAC1 |
| Source | E.coli |
| Protein Expression Range | 1-482aa |
| Tag | N-6His-SUMO |
| Molecular Mass | 71.1kDa |
| Form | Liquid or Lyophilized powder |
| Buffer | Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. |
| Storage | 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C. |
