Histone deacetylase 1/HDAC1 Protein, Human (His-SUMO)

Studies have confirmed that the histone deacetylase 1 (HDAC1) protein is a key enzyme that deacetylates lysine residues on core histones (H2A, H2B, H3, H4). This process establishes an epigenetic repressive signature that affects transcription, cell cycle, and developmental events. Histone deacetylase 1/HDAC1 Protein, Human (His-SUMO) is the recombinant human-derived Histone deacetylase 1/HDAC1 protein, expressed by E. coli , with N-SUMO, N-6*His labeled tag. The total length of Histone deacetylase 1/HDAC1 Protein, Human (His-SUMO) is 482 a.a., with molecular weight of ~71-74 kDa.

Histone deacetylase 1 (HDAC1) Protein serves as a pivotal enzyme that catalyzes the deacetylation of lysine residues located on the N-terminal regions of core histones, including H2A, H2B, H3, and H4. This deacetylation process contributes to the establishment of an epigenetic repression tag and plays crucial roles in transcriptional regulation, cell cycle progression, and developmental events. Functioning within large multiprotein complexes, HDAC1 is a component of the histone deacetylase NuRD complex, actively participating in chromatin remodeling. Beyond histones, HDAC1 exhibits deacetylase activity toward non-histone targets, including NR1D2, RELA, SP1, SP3, and TSHZ3. This versatile enzyme regulates the function of SP proteins (SP1 and SP3) through deacetylation, and it forms part of the BRG1-RB1-HDAC1 complex, which negatively regulates CREST-mediated transcription in resting neurons. Furthermore, HDAC1 acts as a protein decrotonylase, mediating the decrotonylation of histones, thereby expanding its enzymatic repertoire. The multifaceted activities of HDAC1 underscore its central role in epigenetic regulation and diverse cellular processes.

The enzyme activity of this recombinant protein is testing in progress, we cannot offer a guarantee yet.

Human

E. coli

N-SUMO;N-6*His

Q13547 (M1-A482)

3065  [NCBI]

MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA

71-74 kDa

• 
  Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized powder

Lyophilized from 0.2 μm filtered solution in 10 mM Tris-HCl, 1 mM EDTA, 6% Trehalose, pH 8.0 or PBS, 6% Trehalose, pH 7.4 or 20 mM Tris-HCl, 0.5 M NaCl, 6% Trehalose, pH 8.0.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.