货号：15-104

品牌：Merck Millipore

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目录价：￥3261.00

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金山科研平台，产品价格货期咨询微信：jinshanbio Description: Akt/mTOR/S6K Pathway Explorer Antibody MiniPack View All» Promotional Text: Special Offer on Antibodies! Click Here! View All» Trade Name: Upstate (Millipore) View All» Epitope: 05-591SP: PH Domain of Akt09-213SP: phosphorylated Ser2448 of mTOR07-018SP: phosphorylated Ser412/Ser398 of S6K1 and S6K2, respectively View All» Immunogen: 05-591SP: GST-fusion protein corresponding to residues 1-149 of human Akt109-213SP: Synthetic peptide encompassing phosphorylated Ser2448 of human mTOR07-018SP: Synthetic peptide encomopassing phosphorylated Ser412 of p70S6K1 and Ser389 of p70S6K2. View All» Background Information: Pathway Explorer Antibody MiniPack:Each Pathway Explorer Antibody Minipack contains three related antibodies as part of a signaling cascade or a combination of total and phosphorylated forms of key signaling targets. Each of the three antibodies are 30% the original pack size. Full size versions of each of the Pathway Explorer antibodies are available for sale individually under the same catalog number with the removal of “SP” off of each one (e.g. 05-591SP can be ordered as 05-591). Akt:Akt (Protein Kinase B), a Ser/Thr kinase, is a major known effecter of the PI3 Kinase pathway and is involved in multiple signaling pathways that relate to many biological processes including glucose metabolism, cell survival/apoptosis, cell cycle control, angiogenesis, differentiation, and cell growth and proliferation. Akt is activated by ligand-stimulated growth factor receptor signaling that activates the Phosphatidylinositol 3-kinase (PI3 Kinase, PI3K) dependent manner. PKB is one of the most frequently hyperactivated protein kinases in human cancers. In mammals three isoforms of Akt (Akt1/PKBα, Akt2/PKBβ, and Akt3/PKBγ) exists. They exhibit a high degree of homology, but differ slightly in the localization of their regulatory phosphorylation sites. Akt1 is the predominant isoform that is in most tissues and is thought to have a dominant role in growth, survival, embryonic development, and post-natal survival. Additionally, Akt1/PKBα is required for adipocyte differentiation, where as Akt2/PKBβ and Akt3/PKBγ are not. Akt2 is strongly correlated with the regulation of glucose homeostasis and is the predominant PKB isoform expressed in insulin-responsive tissues where defective Akt2 results in impaired insulin-stimulated glucose uptake in muscle and adipocytes. Akt γ is abundant in brain tissue. Each Akt isoform is composed of three functionally distinct regions: an N-terminal Pleckstrin Homology (PH) domain that provides a lipid-binding module to direct Akt to PIP3 at the cell membrane as a result of PI3 Kinase (PI3K) activity that is necessary for its activation, a central catalytic domain, and a C-terminal hydrophobic motif. The activation and regulation of AKT is dependent on a dual regulatory mechanism that requires both its translocation to the plasma membrane and dual phosphorylation on Thr308 and Ser473 by PDK1 and the TORC2 complex, respectively. This is accomplished by the generation and build-up of PIP3 by PI3K in conjunction with reduced PTEN function that results in the activation of PDK1 (3-phosphoinositide-dependent protein kinase-1) and the recruitment of AKT to the plasma membrane by direct interaction with its PH domain. The activated PDK1 then in turn phosphorylates Akt on Thr308 in its activation loop. This phosphorylation is necessary and sufficient for AKT activation; however maximal activation requires the additional phosphorylation at Ser473. Another kinase complex, recently identified as TORC2, which is composed of the mTOR, Rictor, GβL, Sin1, and Protor1 and 2 (previously referred to as the unidentified kinase PDK2), phosphorylates AKT on Ser473 in its hydrophobic motif. After Akt is activated, it is liberated from the plasma membrane and released into the cytosol and nucleus where it interacts with and phosphorylates multiple binding partners. It has been shown to phosphorylate over 40 substrates, some of which are activated by phosphorylation such as mTOR, AS160, PRAS40 (Thr246), IKK, MDM2, NFκB, and TSC1&2 and some that are inhibited by its phosphorylation that include Bad (Ser136), GSK3 (Ser9), FKHR (Ser256), and Caspase 9 (Ser196). Just as these two AKT phosphorylation sites are phosphorylated by two separate mechanisms, they are both regulated by two different phosphatases. The dephosphorylation and subsequent inactivation of AKT is much less understood than its activation. It was not until the recent discovery of two new phosphatases, PHLPP1 and PHLPP2 (PH domain leucine-rich repeat protein phosphatase) that the process was better elucidated. Dephosphorylation of AKT at Ser473, but not at Thr308, was found to be mediated by one or both of the PHLPP family of phosphatases. Another more promiscuous phosphatase, PP2A, is now believed to dephosphorylate AKT on the PDK1 phosphorylation site at Thr308. Together these phosphatases help regulate the activity of AKT. With AKT having so many signaling partners and its involvement in multiple signaling pathways and cellular mechanisms, it is no wonder why AKT is so well studied and a highly sought after drug target.mTOR:mTOR (Mammalian Target of Rapamycin, aka FRAP, RAPT or RAFT) is a large 289 kDa Ser/Thr protein kinase that regulates cell cycle progression, cell growth, protein synthesis, ribosome biogenesis, and autophagy. mTOR is an evolutionarily conserved member of the Phosphoinositol Kinase-related Kinase (PIKK) family whose activity is regulated by phosphorylation on Ser2448 by Akt in response to insulin or muscle activity. Interestingly, mTOR is the central component of two multimeric kinase complexes consisting of mTOR and numerous other mTOR binding proteins. These two multimeric protein complexes are designated mTORC1 and mTORC2. mTORC1 (mTOR Complex 1) consists of at least mTOR, Raptor, and GβL (mLST8). mTORC1 is known to play a central role in insulin signaling, which is crucial in maintaining metabolic homeostasis. The complex is activated primarily though the PI3 Kinase/Akt pathway. Upon insulin stimulation, Akt activates mTORC1 by phosphorylating and inhibiting TSC (and possibly other yet discovered targets and/or mTOR itself). This inhibits the upstream small GTPase regulator Rheb (Ras homolog enriched in brain). This inhibits the kinase activity of the mTORC1 complex, thus disabling its ability to phosphorylate its downstream targets such as p70 S6K on Thr389 and 4E-BP1 on Thr229. The other mTOR complex, mTORC2 (mTOR Complex 2), is made up of at least mTOR, Rictor, GL, Sin1, Protor 1 and 2. mTORC2 affects cell proliferation and survival primarily by phosphorylating the hydrophobic motif of Akt on Ser473, a well-known effecter of the PI3 Kinase pathway. In addition to phosphorylating Akt, the mTORC2 complex is also known to effect cytoskeletal organization and migration by exerting its effects through Rac, Rho, and PKC. Interestingly, unlike mTORC1, the mTORC2 complex appears to not be inhibited by treatment with rapamycin and for this reason is referred to as the rapamycin-insensitive complex. Defects in both mTOR complexes are associated with a variety of diseases, including cancer and diabetes.p70 S6K:S6 Kinase is a Ser/Thr kinase which phosphorylates the 40S ribosomal protein S6, and several translation-regulatory factors. S6 kinase is activated by phosphorylation of multiple sites by mTOR. S6K is an important regulator of protein synthesis, along with MAP Kinase. In neurons, S6K is linked to the cytoskeleton by neurabin, which may play a role in its activation. Rsk3 (MAPKAP Kinase 1c) and Rsk4 are also known as the Ribosomal Protein S6 Kinase, 90 kDa, polypeptide 2 and 6, respectively.*See full size versions for corresponding references. View All» Presentation: 3 individual tubes each containing antibodies directed against one of the three targets; Akt, phosphorylated mTOR, or phosphorylated p70 S6K. View All» UniProt Number: P31749 View All» Entrez Gene Number:

• NM_005163

• NP_004949.1

• NP_003152.1

• NP_003943.2
  View All» Gene Symbol:
  • AKT1

  • RAC

  • PRKBA

  • MGC99656

  • RAC-ALPHA

  • RAC-PK-alpha

  • C-AKT

  • PKB

  • AKT

  • mTOR

  • FRAP

  • FRAP1

  • FRAP2

  • p70 S6K

  • p70 SK1

  • p70 S6K2

  • RPS6KB1

  • S6K1

  • p70 S6K alpha

  • p70 S6K beta

  • S6K2
    View All» Components:
    • 05-591SP Anti-Akt/PKB, PH Domain, clone SKB1; 30 µg

    • 09-213SP Anti-phospho-mTOR (Ser2448); 60 µL

    • 07-018SP Anti-phospho-p70 S6 Kinase I/II (Thr412/Thr397); 30 µg
      View All» Usage Statement: Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals. View All» UniProt Summary: FUNCTION: General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I. Mediates insulin-stimulated protein synthesis, partly by playing a role in both insulin-induced phosphorylation of 4E-BP1 and in insulin-induced activation of p70 S6 kinase. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase. CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. ENZYME REGULATION: Three specific sites, one in the kinase domain (Thr-308) and the two other ones in the C-terminal regulatory region (Ser-473 and Tyr-474), need to be phosphorylated for its full activation. SUBUNIT: Interacts with CENTG1 isoform 2 (PIKE-A) in the presence of guanine nucleotides. The C-terminus interacts with CCDC88A/GRDN and THEM4. Interacts with AKTIP. Interacts (via PH domain) with MTCP1, TCL1A AND TCL1B. Interacts with CDKN1B; the interaction phosphorylates CDKN1B promoting 14-3-3 binding and cell-cycle progression. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Note=Nucleus after activation by integrin-linked protein kinase 1 (ILK1). Nuclear translocation is enhanced by interaction with TCL1A. TISSUE SPECIFICITY: In all human cell types so far analyzed. DOMAIN: Binding of the PH domain to the phosphatidylinositol 3-kinase alpha (PI(3)K) results in its targeting to the plasma membrane. DOMAIN: The AGC-kinase C-terminal mediates interaction with THEM4. PTM: Phosphorylation on Thr-308, Ser-473 and Tyr-474 is required for full activity. Ser-473 phosphorylation by the Rictor-mTor complex favors Thr-308 phosphorylation by PDPK1. Ser-473 phosphorylation is enhanced by interaction with CENTG1 isoform 2 (PIKE-A). Ser-473 phosphorylation is enhanced in focal cortical dysplasias with Taylor-type balloon cells. View All» Brand Family: Upstate View All» Product Name: Akt/mTOR/S6K Pathway Explorer Antibody MiniPack View All» Qty/Pk: 3 vials/Pk View All» Format: Purified View All» Properties: Each vial is 30% the size of the parent catalog number View All»
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