Analytical Data
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Gene name
HDAC3
- Application
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Alternative Names
HDAC3；Histone deacetylase 3
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O15379
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Expression Region
1-428aa
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AA Sequence
MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVINQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVEEAISEELPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLDQIRQTIFENLKMLNHAPSVQIHDVPADLLTYDRTDEADAEERGPEENYSRPEAPNEFYDGDHDNDKESDVEI
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Molecular Weight
52.2kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Identification
Protein Description
Histone deacetylase 3 (HDAC3) is a critical enzyme involved in the regulation of gene expression through chromatin remodeling, impacting various cellular processes such as development, differentiation, and cell cycle progression. HDAC3 operates as part of several multiprotein complexes, influencing the acetylation status of histones and non-histone proteins, thus altering transcriptional activity. Aberrant expression or activity of HDAC3 has been implicated in a variety of diseases, particularly cancer, where it can contribute to the silencing of tumor suppressor genes and the promotion of oncogenic pathways. Consequently, understanding the structural and functional properties of HDAC3 is crucial for developing targeted therapies. Researchers have focused on recombinant expression systems to produce HDAC3 proteins for biochemical and structural studies, enabling the exploration of its catalytic mechanisms, inhibition strategies, and interactions with other cellular factors. Recent advancements in crystallography and cryo-electron microscopy have provided insights into the enzyme's three-dimensional structure, facilitating the design of small-molecule inhibitors with potential therapeutic applications. The ongoing investigation of HDAC3's role in epigenetic regulation also highlights its importance as a therapeutic target in cancer treatment and other diseases associated with dysregulated gene expression. As our understanding of HDAC3 continues to grow, it holds promise for novel strategies in precision medicine, making it a focal point of contemporary biomedical research.
