Application
| WB, IP, ICC |
---|---|
Primary Accession | Q9UBS0 |
Other Accession | NP_003943.2 |
Host | Rabbit |
Reactivity | Human, Mouse, Rat, Bovine |
Clonality | Polyclonal |
Description | Rabbit Anti-Human p70 S6K Polyclonal |
Target/Specificity | Detects ~70kDa. |
Other Names | p70 S6 kinase beta (phospho T229) Antibody, p70-beta Antibody, p70S6Kb Antibody, S6K beta Antibody, S6K2 Antibody, SRK Antibody, STK14B Antibody |
Immunogen | Human p70 S6K c-terminal peptide –KLH conjugates |
Purification | Protein A Purified |
Storage | -20ºC |
Storage Buffer | TBS, 50% glycerol, 0.09% sodium azide |
Shipping Temperature | Blue Ice or 4ºC |
Certificate of Analysis | 0.25 mg/ml was sufficient for detection of SPC-146 in lysates prepared from mouse muscle and mouse brain. |
Cellular Localization | Cytoplasm | Nucleus | Cell Junction | Mitochondrion | Mitochondrion Outer Membrane |
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Provided below are standard protocols that you may find useful for product applications.
Background
Ribosomal S6 (S6K) belongs to the AGC family of Serine/Threonine protein kinases. There are two forms of S6K, alpha and beta, which have cytoplasmic and nuclear variants derived from alternative splicing (1). The activity of S6K is regulated by phosphorylation/ dephosphorylation events in cellular responses to various extracellular stimuli. Its activity has also been shown to be dependent on nutrient availability (3-6). The mechanism of activation of S6K is a multi-step process which is achieved by phosphorylating the 40S ribosomal protein S6, which then upregulates the translation of mRNA transcripts containing an oligopryimidine tract at the 5’ transcriptional start site (3-6). Recently, a highly homologous ribosomal S6 kinase, termed S6K2, was identified. It has 70% amino acid identity in the overall sequence with S6K1, and highly conserved potential phosphorylation sites of S6K1. However, the N- and C-terminal domains of S6K2 are quite different (2). As a result, S6K is a key player in the regulation of cell size, growth and glucose homeostasis.
References
1. Gout, I. et al. (1998). J Biol Chem. 273 (46):30061-30064.
2. Val’Ovka, TI. et al. (2000). Ukr Biokhim Zh. 72(3):31-7.
3. Kawasome, H. et al. (1998) Proc. Natl. Acad.Sci. 95
4. Montagne, J. et al. 1999) Science 285
5. Shima, H. et al. (1998) EMBO J 17: 6649-6659.
6. Lee-Fruman, K. et al. (1999) Oncogene 18: 5108- 5114.