Analytical Data
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Gene name
HDAC1
- Application
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Alternative Names
HDAC1；RPD3L1；Histone deacetylase 1
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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
Q13547
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Expression Region
1-482aa
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AA Sequence
MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA
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Molecular Weight
73.2 kDa
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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 that plays a significant role in the regulation of gene expression by removing acetyl groups from histone and non-histone proteins, leading to chromatin condensation and transcriptional repression. Dysregulation of HDAC1 has been implicated in various diseases, particularly cancer, where its overexpression is associated with tumor progression and poor prognosis. Recent advancements in understanding the structural biology of HDAC1 have paved the way for the development of selective HDAC inhibitors, which hold therapeutic potential in treating malignancies and other HDAC-related disorders. Furthermore, research into the enzymatic mechanisms of HDAC1 is vital for elucidating its diverse biological functions, including its role in cellular differentiation, apoptosis, and the DNA damage response. Recombinant HDAC1 protein has become a valuable tool for in vitro studies, as it allows researchers to investigate its catalytic activity, substrate specificity, and interactions with various co-factors and regulatory proteins. By employing techniques such as X-ray crystallography and nuclear magnetic resonance (NMR), scientists aim to delineate the structural features that govern HDAC1's function, thereby identifying novel targets for drug development. Overall, the study of recombinant HDAC1 protein is essential for advancing our understanding of its role in epigenetics and therapeutics, and it provides insights for designing more effective HDAC inhibitors that can improve clinical outcomes for patients with HDAC-related diseases.
