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Merck

P2859

Sigma-Aldrich

Anti-p300/CBP antibody, Mouse monoclonal

clone NM11, purified from hybridoma cell culture

Sinónimos:

Anti-CREB Binding Protein

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About This Item

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

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

NM11, monoclonal

form

buffered aqueous solution

mol wt

antigen 300 kDa

species reactivity

mouse, rat, human, mink, monkey

concentration

~2 mg/mL

technique(s)

immunocytochemistry: suitable
immunoprecipitation (IP): suitable
microarray: suitable
western blot: 10-20 μg/mL using human 293 embryonal kidney cells

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... KAT2B(8850)
mouse ... Kat2b(18519)
rat ... Pcaf(301164)

General description

Monoclonal Anti-p300/CBP (mouse IgG1 isotype) is derived from the NM11 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a native human p300. The KAT2B (lysine acetyltransferase 2B) gene encodes a p300/CBP (CREB binding protein)-associated factor, which belongs to the family of GNAT (GCN5 (general control nonderepressible 5)-related N-acetyltransferase).

Specificity

Reacts specifically with both p300 and CBP but not with the related p270 molecule. The epitope recognized by the antibody resides within the 21 amino acid stretch spanning amino acids 2071-2091 near the CBP C-terminus. CBP and p300 differ by three noncontiguous residues within this 21 amino acid region, a difference that does not detectably affect the reactivity of the antibody.

Immunogen

native human p300.

Biochem/physiol Actions

p300/CBP are capable of binding to a variety of transcriptional activator and regulatory molecules, including p53 and nuclear hormone receptors. The complexity of these p300/CBP cellular associations suggests that both proteins play a central role in the coordination of gene expression during cell growth and differentiation.
KAT2B (lysine acetyltransferase 2B) possess histone acetyltransferase (HAT) activity and is thus known to regulate transcription process. Acetylation also influences the chromatin structure. Lysine acetylation significantly contributes to protein modification. It is essential for establishing protein function by altering its structure, activity and molecular interaction.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 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

10 - Combustible liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Visite la Librería de documentos

Characterization of monoclonal antibodies raised against p300: both p300 and CBP are present in intracellular TBP complexes.
Dallas P B, et al.
Journal of Virology, 71(2), 1726-1731 (1997)
Adenoviral E1A-associated protein p300 as a functional homologue of the transcriptional co-activator CBP.
Lundblad j R, et al.
Nature, 74(6517), 85-85 (1995)
E1A promotes association between p300 and pRB in multimeric complexes required for normal biological activity.
Wang H G, et al.
Journal of Virology, 69(12), 7917-7924 (1995)
Acetylation regulates DNA repair mechanisms in human cells.
Piekna-Przybylska D, et al.
Cell Cycle, 15(11), 1506-1517 (2016)
Monoclonal Antibody NM11 Recognizes a C-Terminal Epitope Shared by p300 and CBP
Dallas P B, et al.
Hybridoma, 16(3), 273-275 (1997)

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