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H2663

Anti-Histone Deacetylase 2 (HDAC2) antibody, Mouse monoclonal

Name: Anti-Histone Deacetylase 2 (HDAC2) antibody, Mouse monoclonal
Brand: SIGMA

clone HDAC2-62, purified from hybridoma cell culture

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About This Item

MDL number:

MFCD02096544

UNSPSC Code:

12352203

NACRES:

NA.41

biological source

mouse

Quality Level

200

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

HDAC2-62, monoclonal

form

buffered aqueous solution

mol wt

antigen ~55 kDa

species reactivity

human, chicken, bovine, canine, rat, mouse

packaging

antibody small pack of 25 μL

technique(s)

immunohistochemistry: suitable
immunoprecipitation (IP): suitable
indirect ELISA: suitable
microarray: suitable
western blot: 0.25-0.5 μg/mL using total cell extracts from NIH3T3 cells

isotype

IgG2b

UniProt accession no.

Q92769

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... HDAC2(3066)
mouse ... Hdac2(15182)
rat ... Hdac2(84577)

General description

Anti-Histone Deacetylase 2 (HDAC2) antibody, Mouse monoclonal (mouse IgG2b isotype) is derived from the HDAC2-62 hybridoma produced by the fusion of mouse myeloma cells (NS1) and splenocytes from BALB/c mice immunized with a synthetic peptide corresponding to the C-terminal region of human histone deacetylase 2 (amino acid residues with N-terminal added cysteine) conjugated to maleimide-activated KLH. Histone deacetylase 2 (HDAC2) is the catalytic subunits of different multiprotein regulatory complexes.

Specificity

Monoclonal Anti-Histone Deacetylase 2 (HDAC2) recognizes human, bovine, dog, rat, mouse, and chicken HDAC2 (approx. 55 kDa). The antibody epitope resides within amino acids 471-488 of human HDAC2.

Application

Anti-Histone Deacetylase 2 (HDAC2) antibody, Mouse monoclonal has been used in:

co-immunoprecipitation
chromatin immunoprecipitation (ChIP)
western blot
immunohistochemistry
enzyme linked immunosorbent assays (ELISA)

Biochem/physiol Actions

Histone Deacetylases including HDAC′s 1-10 facilitate transcriptional repression and nucleosome condensation. Abnormal recruitment of HDACs by various oncoproteins may occur in certain neoplastic diseases. Inhibition of HDAC2 activity by valproic acid induces proteasomal degradation of HDAC2.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, and 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Dimethyl fumarate regulates histone deacetylase expression in astrocytes

Kalinin S, et al.

Journal of Neuroimmunology, 263 (2013)

Histone deacetylase 2 and N-Myc reduce p53 protein phosphorylation at serine 46 by repressing gene transcription of tumor protein 53-induced nuclear protein 1.

Jeyran Shahbazi et al.

Oncotarget, 5(12), 4257-4268 (2014-06-24)

Myc oncoproteins and histone deacetylases (HDACs) exert oncogenic effects by modulating gene transcription. Paradoxically, N-Myc induces p53 gene expression. Tumor protein 53-induced nuclear protein 1 (TP53INP1) phosphorylates p53 protein at serine 46, leading to enhanced p53 activity, transcriptional activation of

Histone Deacetylases: A Saga of Perturbed Acetylation Homeostasis in Cancer

Parbin S, et al.

The Journal of Histochemistry and Cytochemistry, 62 (2014)

Insights into the activation mechanism of class I HDAC complexes by inositol phosphates

Watson PJ, et al.

Nature Communications, 7 (2016)

Stem Cell Factor SALL4 Represses the Transcriptions of PTEN and SALL1 through an Epigenetic Repressor Complex

Lu J, et al.

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