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AB104121

Recombinant human HDAC1 protein

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Recombinant human HDAC1 protein is a Human Full Length protein, in the 1 to 482 aa range, expressed in Baculovirus, with >50%, suitable for SDS-PAGE, FuncS.

View Alternative Names

RPD3L1, HDAC1, Histone deacetylase 1, HD1, Protein deacetylase HDAC1, Protein deacylase HDAC1

2 Images
Functional Studies - Recombinant human HDAC1 protein (AB104121)
  • FuncS

Supplier Data

Functional Studies - Recombinant human HDAC1 protein (AB104121)

HDAC1 specific activity. HDAC reaction was carried out for 30 minutes at 37°C in a solution containing 25 mM Tris/HCl, pH 8.0, 137 mM NaCl, 2.7 mM KCl, 1 mM MgCl2, 0.1 mg/ml BSA, 20 μM Fluorogenic HDAC substrate, and varying amounts of HDAC1 from 0-80 ng. This was followed by treatment with 50 μL of HDAC developer for 15 minutes at room temperature. Fluorescence intensity is measured at ex360/em460.

SDS-PAGE - Recombinant human HDAC1 protein (AB104121)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant human HDAC1 protein (AB104121)

10% SDS-PAGE showing ab104121 at approximately 56kDa (1μg).

Key facts

Purity

>50% SDS-PAGE

Expression system

Baculovirus

Tags

His tag C-Terminus DDDDK tag C-Terminus

Applications

SDS-PAGE, FuncS

applications

Biologically active

Yes

Biological activity

Specific Activity: 460 pmol/min/μg.

Accession

Q13547

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.754% Sodium chloride, 0.395% Tris HCl, 0.05% Sorbitan monolaurate, ethoxylated

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":"56 kDa","actualMolecularWeight":null,"aminoAcidEnd":482,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q13547","tags":[{"tag":"His","terminus":"C-Terminus"},{"tag":"DDDDK","terminus":"C-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

HDAC1 also known as Histone Deacetylase 1 is a member of the histone deacetylase family with a molecular weight of approximately 55 kDa. Mechanically HDAC1 removes acetyl groups from lysine residues on histone proteins an action known as histone deacetylation. This process causes chromatin structure to become more compact which leads to transcriptional repression. HDAC1 is broadly expressed in various tissues particularly in the brain heart and kidneys and is vital for cellular development and differentiation.
Biological function summary

The enzymatic activity of histone deacetylase effectively controls gene expression. HDAC1 participates as a part of the multiprotein complexes including SIN3 and NuRD which play vital roles in the regulation of transcription. By altering the acetylation state of histones HDAC1 influences chromatin remodeling thereby affecting the accessibility of transcription factors to DNA and controlling genes necessary for cell cycle progression and proliferation.

Pathways

The function of HDAC1 fits into the regulation of the cell cycle and apoptosis pathways. In the cell cycle pathway HDAC1 interacts with other histone deacetylases (HDACs) and plays a role in controlling the progression of the cell division. The interplay between HDAC1 and proteins such as p53 further showcases its regulatory activity in apoptosis ensuring cell survival or programmed cell death when necessary.

HDAC1 shows significant relevance to cancer and neurodegenerative diseases. In cancer the overexpression or abnormal regulation of HDAC1 can lead to uncontrolled cell proliferation often linked to the silencing of tumor suppressor genes. Within neurodegenerative conditions HDAC1-related disturbances in gene expression may result in impaired neuronal function and survival. The involvement of HDAC1 with proteins such as p53 and other HDACs illustrates its impact on complex disease mechanisms making it a critical target for therapeutic interventions.

Specifications

Form

Liquid

Additional notes

Affinity purified.

General info

Function

Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (PubMed : 16762839, PubMed : 17704056, PubMed : 28497810). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed : 16762839, PubMed : 17704056). Histone deacetylases act via the formation of large multiprotein complexes (PubMed : 16762839, PubMed : 17704056). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed : 16428440, PubMed : 28977666). As part of the SIN3B complex is recruited downstream of the constitutively active genes transcriptional start sites through interaction with histones and mitigates histone acetylation and RNA polymerase II progression within transcribed regions contributing to the regulation of transcription (PubMed : 21041482). Also functions as a deacetylase for non-histone targets, such as NR1D2, RELA, SP1, SP3, STAT3 and TSHZ3 (PubMed : 12837748, PubMed : 16285960, PubMed : 16478997, PubMed : 17996965, PubMed : 19343227). Deacetylates SP proteins, SP1 and SP3, and regulates their function (PubMed : 12837748, PubMed : 16478997). Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons (PubMed : 19081374). Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation (PubMed : 19081374). Deacetylates TSHZ3 and regulates its transcriptional repressor activity (PubMed : 19343227). Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B (PubMed : 17000776). Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity (PubMed : 17996965). Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development (By similarity). Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator : CLOCK-BMAL1 heterodimer (By similarity). Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation (By similarity). In addition to protein deacetylase activity, also has protein-lysine deacylase activity : acts as a protein decrotonylase and delactylase by mediating decrotonylation ((2E)-butenoyl) and delactylation (lactoyl) of histones, respectively (PubMed : 28497810, PubMed : 35044827).

Sequence similarities

Belongs to the histone deacetylase family. HD type 1 subfamily.

Post-translational modifications

Sumoylated on Lys-444 and Lys-476; which promotes enzymatic activity. Desumoylated by SENP1.. Phosphorylation on Ser-421 and Ser-423 promotes enzymatic activity and interactions with NuRD and SIN3 complexes. Phosphorylated by CDK5.. Ubiquitinated by CHFR, leading to its degradation by the proteasome. Ubiquitinated by KCTD11, leading to proteasomal degradation.

Subcellular localisation

Nucleus

Product protocols

Target data

Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (PubMed : 16762839, PubMed : 17704056, PubMed : 28497810). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed : 16762839, PubMed : 17704056). Histone deacetylases act via the formation of large multiprotein complexes (PubMed : 16762839, PubMed : 17704056). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed : 16428440, PubMed : 28977666). As part of the SIN3B complex is recruited downstream of the constitutively active genes transcriptional start sites through interaction with histones and mitigates histone acetylation and RNA polymerase II progression within transcribed regions contributing to the regulation of transcription (PubMed : 21041482). Also functions as a deacetylase for non-histone targets, such as NR1D2, RELA, SP1, SP3, STAT3 and TSHZ3 (PubMed : 12837748, PubMed : 16285960, PubMed : 16478997, PubMed : 17996965, PubMed : 19343227). Deacetylates SP proteins, SP1 and SP3, and regulates their function (PubMed : 12837748, PubMed : 16478997). Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons (PubMed : 19081374). Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation (PubMed : 19081374). Deacetylates TSHZ3 and regulates its transcriptional repressor activity (PubMed : 19343227). Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B (PubMed : 17000776). Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity (PubMed : 17996965). Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development (By similarity). Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator : CLOCK-BMAL1 heterodimer (By similarity). Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation (By similarity). In addition to protein deacetylase activity, also has protein-lysine deacylase activity : acts as a protein decrotonylase and delactylase by mediating decrotonylation ((2E)-butenoyl) and delactylation (lactoyl) of histones, respectively (PubMed : 28497810, PubMed : 35044827).
See full target information HDAC1

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