Phospho–p70 S6k (S235/236)
Cat Number: | ABP-0538 |
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Conjugate: | Unconjugated |
Size: | 100 ug |
Clone: | Poly |
Concentration: | 1mg/ml |
Host: | Rb |
Isotype: | IgG |
Immunogen: | A synthetic phosphorylated peptide around S235 & S236 of human RPS6. |
Reactivity: | Hu |
Applications: | Western Blot: 1:500 – 1:2000 |
Molecular Weight: | 32KDa |
Synonyms: | RPS6;S6;RPS6 |
Background: | Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a cytoplasmic ribosomal protein that is a component of the 40S subunit. The protein belongs to the S6E family of ribosomal proteins. It is the major substrate of protein kinases in the ribosome, with subsets of five C-terminal serine residues phosphorylated by different protein kinases. Phosphorylation is induced by a wide range of stimuli, including growth factors, tumor-promoting agents, and mitogens. Dephosphorylation occurs at growth arrest. The protein may contribute to the control of cell growth and proliferation through the selective translation of particular classes of mRNA. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. |
Form: | liquid |
Buffer: | PBS with 0.02% sodium azide, 50% glycerol, pH7.3. |
Storage: | Store at -20℃. Avoid freeze / thaw cycles. |
Western blot analysis of extracts of various cell lines, using Phospho-S6 Ribosomal Protein (RPS6)-S235/236 antibody at 1:1000 dilution.HeLa cells NIH/3T3 cells and PC-12 cells were treated by 10% FBS at 37℃ for 30 minutes after serum-starvation overnight.NIH/3T3 cells were treated by PDGF (100 ng/ml) at 37℃ for 30 minutes after serum-starvation overnight. Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) at 1:10000 dilution. Lysates/proteins: 25ug per lane. Blocking buffer: 3% nonfat dry milk in TBST. Detection: ECL West Pico Plus. Exposure time: 1s.