SRP2072
HDAC3 human
recombinant, expressed in insect cells, ≥70% (SDS-PAGE)
Synonym(s):
HD3, RPD3, RPD3-2
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About This Item
UNSPSC Code:
12352200
NACRES:
NA.26
Recommended Products
biological source
human
recombinant
expressed in insect cells
assay
≥70% (SDS-PAGE)
form
frozen liquid
mol wt
~50 kDa
packaging
pkg of 5 μg
storage condition
avoid repeated freeze/thaw cycles
concentration
300 μg/mL
color
colorless to clear
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... HDAC3(8841)
Biochem/physiol Actions
The nucleosomal histones can be modified through reversible acetylation by histone acetyltransferases (HATs) and deacetylases (HDACs). Acetylation and deacetylation of histone proteins alters chromosome structure and affects transcription factor access to DNA. HDAC3 has an open reading frame of 428 amino acids. HDAC3 shares 53 % amino acid identity with HDAC1 and 52 % with HDAC2. Observations indicate that class II HDACs regulate transcription by bridging the enzymatically active NCOR2-HDAC3 complex and select transcription factors. All HDACs were found to be ubiquitously expressed in immune and non-immune tissues. In human myeloid leukemia THP-1 cells, HDAC3 transfection resulted in increased size, aberrant nuclear morphology and cell cycle G2/M cell accumulation. Functional activity of the expressed HDAC3 protein was confirmed in alpha-HDAC3 antibody immunoprecipitates by a histone deacetylase assay. Study suggests the participation of HDACs in cell cycle progression and activation.
Physical form
Clear and colorless frozen liquid solution
Preparation Note
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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F Dangond et al.
Biochemical and biophysical research communications, 242(3), 648-652 (1998-02-17)
The nucleosomal histones can be modified through reversible acetylation by histone acetyltransferases (HATs) and deacetylases (HDACs). HATs induce nucleosomal relaxation and allow DNA-binding by transcriptional activators. HDACs from corepressor complexes which negatively regulate cell growth. However, the HDAC inhibitors butyrate
Rachel Fellows et al.
Nature communications, 9(1), 105-105 (2018-01-11)
The recently discovered histone post-translational modification crotonylation connects cellular metabolism to gene regulation. Its regulation and tissue-specific functions are poorly understood. We characterize histone crotonylation in intestinal epithelia and find that histone H3 crotonylation at lysine 18 is a surprisingly
W M Yang et al.
The Journal of biological chemistry, 272(44), 28001-28007 (1997-11-05)
Several human cDNAs encoding a histone deacetylase protein, HDAC3, have been isolated. Analysis of the predicted amino acid sequence of HDAC3 revealed an open reading frame of 428 amino acids with a predicted molecular mass of 49 kDa. The HDAC3
Hemangi Patil et al.
The Journal of biological chemistry, 291(7), 3158-3172 (2015-12-15)
Histone deacetylase 3 (HDAC3) and linker histone H1 are involved in both chromatin compaction and the regulation of mitotic progression. However, the mechanisms by which HDAC3 and H1 regulate mitosis and the factors controlling HDAC3 and H1 activity during mitosis
David E Wright et al.
Antioxidants & redox signaling, 29(4), 377-388 (2017-11-10)
Thioredoxin reductase 1 (TrxR1) is a cancer target and essential selenoprotein that defends the cell against reactive oxygen species and regulates cellular signaling and redox pathways. Previous cell-based studies correlated TrxR1 acetylation with modulated cellular reduction activity, yet the function
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