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Cat. No.: DPP-001102
| Product Overview | |
|---|---|
| Species | Human |
| Expression System | Baculovirus infected insect cells |
| Endotoxin Level | < 1.000 Eu/µg |
| Format | Liquid |
| Purity | ≥ 98% by HPLC |
| Nature | Recombinant |
| Target Information | |
|---|---|
| Gene Name | RPS6KB1 |
| UniProt No. | P23443 |
| Gene ID | 6198 |
| Molecular Weight | 60 kDa including tags |
| Alternative Names | 70 kDa ribosomal protein S6 kinase 1; KS6B1_HUMAN; p70 alpha; P70 beta 1; p70 ribosomal S6 kinase alpha; p70 ribosomal S6 kinase beta 1; P70 S6 Kinase; p70 S6 kinase alpha; p70 S6 kinase, alpha 1; p70 S6 kinase, alpha 2; p70 S6K; p70 S6K-alpha; p70 S6KA; p70(S6K) alpha; p70(S6K)-alpha; p70-alpha; p70-S6K; p70-S6K 1; P70S6K; P70S6K1; p70S6Kb; PS6K; Ribosomal protein S6 kinase 70kDa polypeptide 1; Ribosomal protein S6 kinase beta 1; Ribosomal protein S6 kinase beta-1; Ribosomal protein S6 kinase I; RPS6KB1; S6K; S6K-beta-1; S6K1; Serine/threonine kinase 14 alpha; Serine/threonine-protein kinase 14A; STK14A |
| Function | Acts 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. |
| Cellular Localization | Cytoplasm; Nucleus. Cytoplasm and Cell junction > synapse > synaptosome. Mitochondrion outer membrane. |
| Protein Length | Full length protein |
| Sequence | MRRRRRRDGFYPAPDFRDREAEDMAGVFDIDLDQPEDAGSEDELEEGGQL NESMDHGGVGPYELGMEHCEKFEISETSVNRGPEKIRPECFELLRVLGKG GYGKVFQVRKVTGANTGKIFAMKVLKKAMIVRNAKDTAHTKAERNILEEV KHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLA EISMALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVT HTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPFTGENRKK TIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHP FFRHINWEELLARKVEPPFKPLLQSEEDVSQFDSKFTRQTPVDSPDDSTL SESANQVFLGFTYVAPSVLESVKEKFSFEPKIRSPRRFIGSPRTPVSPVK FSPGDFWGRGASASTANPQTPVEYPMETSGIEQMDVTMSGEASAPLPIRQ PNSGPYKKQAFPMISKRPEHLRMNLLEHHHHHH,Belongs 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. |
| Shipping & Storage | |
|---|---|
| Shipping | Shipped on dry ice. |
| Storage | Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle. |
Ace Therapeutics has a team of experts in the field of endocrine and metabolic research, aiming to provide innovative preclinical contract research solutions to cope with diabetes and its complications. We provide customized solutions and technical support, enabling the transformation of promising concepts into innovative treatments, thus accelerating the drug development process of diabetes.
