Anti-Phospho-S6K-Ser398 antibody (STJA0003773)
SPECIFICATIONS
ClonalityPolyclonal
HostRabbit
ConjugationUnconjugated
IsotypeIgG
ImmunogenSynthetic phospho-peptide corresponding to amino acid residues surrounding Thr398 conjugated to KLH.
General Information
| Short Description | Rabbit polyclonal anti-Phospho-p70 S6 Kinase-Ser398 for use in WB in D.melanogaster samples. Datasheet included with dilution recommendations, and related reagents. |
| Applications | WB |
| Host | Rabbit |
| Reactivity | D.melanogaster |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Clonality | Polyclonal |
| Isotype | IgG |
| Conjugation | Unconjugated |
| Purification | This antibody was antigen affinity purified from pooled serum. |
| Dilution Range | WB 1:1000 |
| Formulation | 100 ยตl in 10 mM HEPES (pH 7.5) , 150 mM NaCl, 100 ยตg per ml BSA and 50% Glycerol. |
| Storage Instruction | Store at-20ยฐC for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles. |
Target Information
| Immunogen | Synthetic phospho-peptide corresponding to amino acid residues surrounding Thr398 conjugated to KLH. |
Additional Info
| Background | p70 S6 kinase (p70 S6K) is activated in a signaling pathway that includes mTOR and is a mitogen-activated Ser/Thr protein kinase that is required for cell growth and G1 cell cycle progression (Xio et al., 2009). p70 S6K is controlled by multiple phosphorylation events located within the catalytic, linker and pseudosubstrate domains and subsequently phosphorylates specifically ribosomal protein S6 (Saitoh et al., 229 389 2002). Phosphorylation of Thr in the catalytic domain and Thr in the linker domain are most critical for kinase function. Inhibition of p70 activity inhibits the entry into S phase of the cell cycle and exhibits cell cycle arrest at G0/G1 phase, suggesting that the activation of p70 S6k plays an obligatory role in mediating mitogenic signals during cell activation (Xio et al., 2009). |
Information sourced from Uniprot.org