Analytical Data
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Gene name
Histone deacetylase 1/HDAC1
- Application
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Alternative Names
HDAC1; GON10; HD1; RPD3; RPD3L1
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q13547
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Expression Region
Met1~Ala482
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Molecular Weight
22&70kDa
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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
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Protein Description
Histone deacetylase 1 (HDAC1) is a crucial enzyme involved in the regulation of gene expression through the removal of acetyl groups from lysine residues on histone proteins, leading to chromatin condensation and transcriptional repression. Aberrant HDAC1 activity has been implicated in various pathological conditions, including cancer, neurodegenerative disorders, and cardiovascular diseases. Researchers have recognized the potential of HDAC1 as a therapeutic target, prompting the need for a deeper understanding of its structure and function. The development of recombinant HDAC1 proteins has facilitated advanced studies into its enzymatic mechanisms, substrate specificity, and interactions with other molecular partners. These recombinant proteins can be used in various assays, including enzyme activity tests and drug screening, providing insights into HDAC1's role in cellular processes. Additionally, understanding HDAC1's structure can help in the design of selective inhibitors that could serve as novel therapeutics. Recent advances in protein expression and purification techniques have enabled the generation of high-purity HDAC1, fostering research aimed at unraveling its complex functions and contributions to disease. Overall, the study of recombinant HDAC1 highlights its significance in epigenetic regulation and underscores the continuing exploration of therapeutic strategies targeting HDACs in various disease contexts.
