The c-Jun protein is a major component of the transcription factor AP-1, originally shown to mediate phorbol ester tumor promoter (TPA)-induced expression of responsive genes through the TPA-response element (TRE). The Jun proteins form homo- and heterodimers which bind the TRE, while Fos proteins are active only as heterodimers with any of the Jun proteins. Fos/Jun heterodimers have a much higher affinity for the TRE than Jun homodimers. A distant member of the MAP kinase family, designated c-Jun NH2-terminal kinase (JNK1) functions to regulate c-Jun by phosphorylation at the amino terminal serine regulatory sites, Ser 63 and Ser 73). RPL10 has been described as a transcription factor that can function to bind DNA directly or alternatively can interact with c-Jun to inhibit transactivation of AP-1 promoter driven reporter vectors by Jun-Jun homodimers. RPL10 is highly conserved throughout eukaryotic evolution and is apparently a member of a multi-gene family.

60S ribosomal protein L10; Laminin receptor homolog; Protein QM; Tumor suppressor QM; DXS648E; QM

p27635

Human,Mouse,Rat

WB

WB 1:500-1:1000

~ 25 kDa

Rabbit

This antibody detects endogenous levels of RPL10 protein.

Synthetic peptide, corresponding to the N-terminal of Human RPL10.

Polyclonal

Rabbit IgG

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

PBS with 0.02% sodium azide, 50% glycerol, pH7.2

1mg/ml

Store at 4℃ short term,and store at -20℃ long term. Avoid freeze-thaw cycles.