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H2663

Sigma-Aldrich

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

clone HDAC2-62, purified from hybridoma cell culture

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

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.

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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Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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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HDAC2 Inhibitor Valproic Acid Increases Radiation Sensitivity of Drug-Resistant Melanoma Cells
Kalal BS, et al.
Medical sciences (Basel, Switzerland), 7 (2019)
Combined HDAC1 and HDAC2 Depletion Promotes Retinal Ganglion Cell Survival After Injury Through Reduction of p53 Target Gene Expression
Lebrun-Julien F and Suter U
ASN Neuro, 7 (2015)
Stem Cell Factor SALL4 Represses the Transcriptions of PTEN and SALL1 through an Epigenetic Repressor Complex
Lu J, et al.
PLoS ONE, 4 (2009)
Christi Cho et al.
International journal of molecular sciences, 23(3) (2022-02-16)
Epilepsy is a heterogenous neurological disorder characterized by recurrent unprovoked seizures, mitochondrial stress, and neurodegeneration. Hydrogen sulfide (H2S) is a gasotransmitter that promotes mitochondrial function and biogenesis, elicits neuromodulation and neuroprotection, and may acutely suppress seizures. A major gap in
Insights into the activation mechanism of class I HDAC complexes by inositol phosphates
Watson PJ, et al.
Nature Communications, 7 (2016)

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