Anti-S6K1 (phospho S418) antibody (ab58534)
- Product nameAnti-S6K1 (phospho S418) antibodySee all S6K1 primary antibodies ...
- DescriptionRabbit polyclonal to S6K1 (phospho S418)
- Specificityab58534 detects endogenous levels of S6K only when phosphorylated at serine 418.
- Tested applicationsELISA, IHC-P more details
- Species reactivityReacts with: Human
Predicted to work with: Mouse, Rat
Synthetic phosphopeptide derived from human S6K around the phosphorylation site of serine 418 (I-G-SP-P-R).
- Positive controlHuman breast carcinoma.
- Storage instructionsStore at -20°C. Stable for 12 months at -20°C
- Storage bufferPreservative: 0.02% Sodium Azide
Constituents: 50% Glycerol, PBS (without Mg2+ and Ca2+), 150mM Sodium chloride, pH 7.4
- Concentration information loading...
- PurityImmunogen affinity purified
- Purification notesab58534 was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
- Clonality Polyclonal
- Research Areas
Our Abpromise guarantee covers the use of ab58534 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|IHC-P||IHC-P: Use at an assay dependent dilution.|
- FunctionActs to integrate nutrient and growth factor signals in regulation of protein synthesis, cell proliferation, cell growth, cell cycle progression and cell survival. Downstream effector of the mTOR signaling pathway. Phosphorylates specifically ribosomal protein S6 in response to insulin or several classes of mitogens. During translation initiation, the inactive form associatess with the eIF-3 complex under conditions of nutrient depletion. Mitogenic stimulation leads to phosphorylation and dissociation from the eIF-3 complex and the free activated form can phosphorylate other translational targets including EIF4B. Promotes protein synthesis by phosphorylating PDCD4 at 'Ser-67' and targeting it for degradation. Phosphorylates RICTOR leading to regulation of mammalian target of rapamycin complex 2 (mTORC2) signaling; probably phosphorylates RICTOR at 'Thr-1135'. Phosphorylates IRS1 at multiple serine residues coupled with insulin resistance; probably phosphorylates IRS1 at 'Ser-270'. Required for TNF-alpha induced IRS-1 degradation. Phosphorylates EEF2K in response to IGF1 and inhibits EEF2K activity. Phosphorylates BAD at 'Ser-99' in response to IGF1 leading to BAD inactivation and inhibition of BAD-induced apoptosis. Phosphorylates mitochondrial RMP leading to dissociation of a RMP:PPP1CC complex; probably phosphorylates RMP at 'Ser-99'. The free mitochondrial PPP1CC can dephosphorylate RPS6KB1 at Thr-412 which is proposed to be a negative feed back mechanism for the RPS6KB1 antiapoptotic function. Phosphorylates GSK3B at 'Ser-9' under conditions leading to loss of the TSC1-TSC2 complex. Phosphorylates POLDIP3.
- Tissue specificityWidely expressed.
- Sequence similaritiesBelongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. S6 kinase subfamily.
Contains 1 AGC-kinase C-terminal domain.
Contains 1 protein kinase domain.
- DomainThe autoinhibitory domain is believed to block phosphorylation within the AGC-kinase C-terminal domain and the activation loop.
The TOS (TOR signaling) motif is essential for activation by mTORC1.
modificationsPhosphorylation at Thr-412 is regulated by mTORC1. The phosphorylation at this site is maintained by an agonist-dependent autophosphorylation mechanism.
- Cellular localizationCytoplasm; Nucleus. Cytoplasm and Cell junction > synapse > synaptosome. Mitochondrion outer membrane.
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Anti-S6K1 (phospho S418) antibody images
ab58534 at 1/50 dilution staining S6K in human breast carcinoma by Immunohistochemistry, Paraffin embedded tissue, in the absence or presence of the immunising peptide.
References for Anti-S6K1 (phospho S418) antibody (ab58534)
ab58534 has not yet been referenced specifically in any publications.