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In the production of recombinant Human HDAC1 protein, the gene for HDAC1 (E.coli) was cloned into a vector and expressed as HDAC1 protein in E.coli. The plasmids with the copy of HDAC1, or the expression vector, were often used to enhance gene expression. Every step of production was undergone with a strict QC system. N-terminal 6xHis-SUMO tag was used in the process. The purity is 90% determined by SDS-PAGE.HDAC1 belongs to the class IV family. HDAC1 is found in at least three evolutionally conserved, distinct protein complexes: the Sin3, the CoREST and the Mi-2/NuRD complexes. HDAC1 activity is modulated through various post translational modifications including phosphorylation, acetylation, ubiquitination, sumoylation, and nitrosylation. HDAC1 is phosphorylated at serine 421 and 423 by casein kinase II and dephosphorylated by mitogen-activated protein kinase phosphatase-3 (MKP-3). Mutagenesis analysis suggested that phosphorylation on these sites are important for histone deacetylase activity and for HDAC1 to interact with corepressor complexes. HDAC1 phosphorylation increases during the G1 phase and was significantly reduced during the late S/G2 phase. Clinically, it has been shown HDACi can reactivate fetal globin in adult erythroid cells, suggesting the role of HDAC1 in modulating key transcription factors for erythropoiesis and its clinical relevance.
In the production of recombinant Human HDAC1 protein, the gene for HDAC1 (E.coli) was cloned into a vector and expressed as HDAC1 protein in E.coli. The plasmids with the copy of HDAC1, or the expression vector, were often used to enhance gene expression. Every step of production was undergone with a strict QC system. N-terminal 6xHis-SUMO tag was used in the process. The purity is 90% determined by SDS-PAGE.HDAC1 belongs to the class IV family. HDAC1 is found in at least three evolutionally conserved, distinct protein complexes: the Sin3, the CoREST and the Mi-2/NuRD complexes. HDAC1 activity is modulated through various post translational modifications including phosphorylation, acetylation, ubiquitination, sumoylation, and nitrosylation. HDAC1 is phosphorylated at serine 421 and 423 by casein kinase II and dephosphorylated by mitogen-activated protein kinase phosphatase-3 (MKP-3). Mutagenesis analysis suggested that phosphorylation on these sites are important for histone deacetylase activity and for HDAC1 to interact with corepressor complexes. HDAC1 phosphorylation increases during the G1 phase and was significantly reduced during the late S/G2 phase. Clinically, it has been shown HDACi can reactivate fetal globin in adult erythroid cells, suggesting the role of HDAC1 in modulating key transcription factors for erythropoiesis and its clinical relevance.
| Cat.No | ACP04065 | Target Name | HDAC1 |
|---|---|---|---|
| Target Synonyms | DKFZp686H12203; GON 10; HD1; HDAC 1; HDAC1; HDAC1_HUMAN; Histone deacetylase 1; Reduced potassium dependency yeast homolog like 1; RPD3; RPD3L1 | Form | Liquid or Lyophilized powder |
| Expression System | E.coli | Expression Range | 1-482aa |
| Mol Weight | 71.1kDa | Protein Length | Full length |
| Purity | Greater than 90% as determined by SDS-PAGE. | Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | Q13547 |
|---|
Uniprot Id
Q13547
Target Species
Human
Target Name
HDAC1
Target Full Name
Histone deacetylase 1
Target Function
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation.
Target Subcellular Location
Nucleus.
Target Protein Families
Histone deacetylase family, HD type 1 subfamily
Target Tissue Specificity
Ubiquitous, with higher levels in heart, pancreas and testis, and lower levels in kidney and brain.
Target Research Area
Immunology
Target Synonyms
DKFZp686H12203; GON 10; HD1; HDAC 1; HDAC1; HDAC1_HUMAN; Histone deacetylase 1; Reduced potassium dependency yeast homolog like 1; RPD3; RPD3L1
Target Background
Histone acetylation and deacetylation, catalyzed by multisubunit complexes, play a key role in the regulation of eukaryotic gene expression. The protein encoded by this gene belongs to the histone deacetylase/acuc/apha family and is a component of the histone deacetylase complex. It also interacts with retinoblastoma tumor-suppressor protein and this complex is a key element in the control of cell proliferation and differentiation. Together with metastasis-associated protein-2, it deacetylates p53 and modulates its effect on cell growth and apoptosis.
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