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GBL Antibody (ascites)

Mouse Monoclonal Antibody (Mab)

     
  • WB - GBL Antibody (ascites) AM1904A
    GBL (Cat. #AM1904a) western blot analysis in mouse testis tissue lysates (35μg/lane).This demonstrates the GBL antibody detected the GBL protein (arrow).
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  • SPECIFICATION
  • CITATIONS
  • PROTOCOLS
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Product Information
Application
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • E=ELISA
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immuno electron microscopy
  • EIA=Enzyme Immunoassay
WB, E
Primary Accession Q9BVC4
Other Accession NP_071767.3
Reactivity Mouse
Host Mouse
Clonality Monoclonal
Isotype IgG1,k
Clone/Animal Names 211CT7.1.1
Calculated MW 35876 Da
Additional Information
Gene ID 64223
Other Names Target of rapamycin complex subunit LST8, TORC subunit LST8, G protein beta subunit-like, Gable, Protein GbetaL, Mammalian lethal with SEC13 protein 8, mLST8, MLST8, GBL, LST8
Target/Specificity This GBL monoclonal antibody is generated from mouse immunized with GBL recombinant protein.
Dilution WB~~1:100~8000
Format Mouse monoclonal antibody supplied in crude ascites with 0.09% (W/V) sodium azide.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsGBL Antibody (ascites) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name MLST8 {ECO:0000303|PubMed:34741373, ECO:0000312|HGNC:HGNC:24825}
Function Subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals (PubMed:12718876, PubMed:15268862, PubMed:15467718, PubMed:24403073). mTORC1 is activated in response to growth factors or amino acids (PubMed:12718876, PubMed:15268862, PubMed:15467718, PubMed:24403073). In response to nutrients, mTORC1 is recruited to the lysosome membrane and promotes protein, lipid and nucleotide synthesis by phosphorylating several substrates, such as ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) (PubMed:12718876, PubMed:15268862, PubMed:15467718, PubMed:24403073). In the same time, it inhibits catabolic pathways by phosphorylating the autophagy initiation components ULK1 and ATG13, as well as transcription factor TFEB, a master regulators of lysosomal biogenesis and autophagy (PubMed:24403073). The mTORC1 complex is inhibited in response to starvation and amino acid depletion (PubMed:24403073). Within mTORC1, LST8 interacts directly with MTOR and enhances its kinase activity (PubMed:12718876). In nutrient-poor conditions, stabilizes the MTOR- RPTOR interaction and favors RPTOR-mediated inhibition of MTOR activity (PubMed:12718876). mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive (PubMed:15467718). mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors (PubMed:15467718). mTORC2 promotes the serum-induced formation of stress-fibers or F-actin (PubMed:15467718). mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation (PubMed:15467718). mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422' (PubMed:15467718). mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657' (PubMed:15467718).
Cellular Location Lysosome membrane. Cytoplasm {ECO:0000250|UniProtKB:Q9Z2K5}. Note=Targeting to lysosomal membrane depends on amino acid availability: mTORC1 is recruited to lysosome membranes via interaction with GTP-bound form of RagA/RRAGA (or RagB/RRAGB) in complex with the GDP-bound form of RagC/RRAGC (or RagD/RRAGD), promoting its mTORC1 recruitment to the lysosomes
Tissue Location Broadly expressed, with highest levels in skeletal muscle, heart and kidney.
Research Areas
Citations (0)
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Background

Subunit of both mTORC1 and mTORC2, which regulate cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino-acids. Amino-acid-signaling to mTORC1 is mediated by Rag GTPases, which cause amino-acid-induced relocalization of mTOR within the endomembrane system. Growth factor-stimulated mTORC1 activation involves AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Within mTORC1, LST8 interacts directly with FRAP1 and enhances its kinase activity. In nutrient-poor conditions, stabilizes the FRAP1-RPTOR interaction and favors RPTOR-mediated inhibition of FRAP1 activity. mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'.

References

Ali, S.M., et al. J. Biol. Chem. 280(20):19445-19448(2005)
Inoki, K., et al. Microbiol. Mol. Biol. Rev. 69(1):79-100(2005)
Sarbassov, D.D., et al. Science 307(5712):1098-1101(2005)
Jacinto, E., et al. Nat. Cell Biol. 6(11):1122-1128(2004)
Kim, D.H., et al. Mol. Cell 11(4):895-904(2003)

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$ 182.50
Cat# AM1904A
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