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Merck
CN

06-225

Anti-c-Jun Antibody

serum, Upstate®

Synonym(s):

Activator protein 1, AP1, p39, Proto-oncogene c-Jun, Transcription factor AP-1, V-jun avian sarcoma virus 17 oncogene homolog

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
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Product Name

Anti-c-Jun Antibody, serum, Upstate®

biological source

rabbit

conjugate

unconjugated

antibody form

serum

antibody product type

primary antibodies

clone

polyclonal

species reactivity

human, avian, mouse

manufacturer/tradename

Upstate®

technique(s)

immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable

isotype

IgG

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Quality Level

Gene Information

human ... JUN(3725)
mouse ... Jun(16476)

Physical form

Whole rabbit antiserum containing 0.05% sodium azide
Antiserum

Preparation Note

2 years at -20°C

Analysis Note

Control
Positive Antigen Control: Catalog #12-303, Jurkat cell lysate.
routinely evaluated by immunoblot on RIPA lysates from human A431 cells or in Jurkat cell lysate

Application

Detect c-Jun, also known as transcription factor AP-1, with Anti-c-Jun rabbit polyclonal antiserum, Cat. No. 06-225, that has been demonstrated to work in Immunocytochemistry, Immunoprecipitation, and Western blotting.
Research Category
Epigenetics & Nuclear Function
Research Sub Category
Transcription Factors

Biochem/physiol Actions

c-Jun

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.

General description

35-39 kDa
c-Jun is a component of the transcription factor AP-1 that binds and activates transcription at TRE/AP-1 elements and appears to be a major downstream target of the SAPK/JNK signaling pathway. The transcriptional activity of c-Jun is regulated by phosphorylation at Ser63 and Ser73. Extracellular signals including growth factors, transforming oncoproteins and UV irradiation stimulate phosphorylation of c-Jun at Ser63/73 and activate c-Jun dependent transcription. Mutation of Ser63/73 renders c-Jun nonresponsive to mitogenic and stress induced
signaling pathways. The MAP kinase homologue, SAPK/JNK, binds to the N-terminal region of c-Jun and phosphorylates c-Jun at Ser63/73. In addition, the activity of SAPK/JNK is stimulated by the same signals that activate c-Jun.

Immunogen

Trp E fusion-protein containing the DNA binding domain of avian c-Jun

Other Notes

Replaces: 04-210

Legal Information

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

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Storage Class

10 - Combustible liquids

wgk

WGK 1


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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Characterization of the chromosomal binding sites and dimerization partners of the viral oncoprotein Meq in Marek's disease virus-transformed T cells.
Alon M Levy, Yoshihiro Izumiya, Peter Brunovskis, Liang Xia, Mark S Parcells et al.
Journal of virology null
The role of activating protein 1 in the transcriptional regulation of the human FCGR2B promoter mediated by the -343 G -> C polymorphism associated with systemic lupus erythematosus.
Olferiev, M; Masuda, E; Tanaka, S; Blank, MC; Pricop, L
The Journal of Biological Chemistry null
Multiple mitogen-activated protein kinases are regulated by hyperosmolality in mouse IMCD cells.
T Berl, G Siriwardana, L Ao, L M Butterfield, L E Heasley, T Berl, G Siriwardana, L Ao et al.
The American Journal of Physiology null
The oncogenic microRNA OncomiR-21 overexpressed during Marek's disease lymphomagenesis is transactivated by the viral oncoprotein Meq.
Stik, G; Dambrine, G; Pfeffer, S; Rasschaert, D
Journal of virology null
Myristylation alters DNA-binding activity and transactivation of FBR (gag-fos) protein
Kamata, N., et al
Molecular and cellular biology, 11, 765-772 (1991)

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