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AB231487

Anti-HDAC1 antibody - C-terminal

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(1 Publication)

Rabbit Polyclonal HDAC1 antibody. C-terminal. Suitable for IHC-P and reacts with Human samples. Cited in 1 publication.

View Alternative Names

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

1 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-HDAC1 antibody - C-terminal (AB231487)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-HDAC1 antibody - C-terminal (AB231487)

Formalin-fixed, paraffin-embedded human breast carcinoma tissue stained for HDAC1 using ab231487 at 1/200 dilution in immunohistochemical analysis.

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IHC-P

applications

Immunogen

The exact immunogen used to generate this antibody is proprietary information.

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.6 Preservative: 0.1% Sodium azide Constituents: PBS, 1% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

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.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

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, ZNF76 and TSHZ3 (PubMed : 12837748, PubMed : 16285960, PubMed : 16337145, 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

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Journal of vascular research 55:255-267 PubMed30179877

2018

Perfusion Tissue Culture Initiates Differential Remodeling of Internal Thoracic Arteries, Radial Arteries, and Saphenous Veins.

Applications

Unspecified application

Species

Unspecified reactive species

David A Prim,Vinal Menon,Shahd Hasanian,Laurel Carter,Tarek Shazly,Jay D Potts,John F Eberth
View all publications

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