Anti-MTOR (C-terminal) polyclonal antibody

Name: Anti-MTOR (C-terminal) polyclonal antibody
SKU: DPABH-00361
Rating: 5 (1 reviews)

Rabbit Anti-Human MTOR (C-terminal) polyclonal antibody for WB, IHC-P

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COA

SDS

Datasheet

Summary

Specifications

Antibody Isotype

IgG

Species Reactivity

Mouse; Rat; Human

Immunogen

Recombinant fragment, corresponding to a region within C terminal amino acids 2386-2549 of Human mTOR (P42345).

Conjugate

Unconjugated

Applications

Application Notes

WB: 1/500 - 1/3000; IHC-P: 1/100 - 1/1000.

Target

Alternative Names

MTOR; mechanistic target of rapamycin (serine/threonine kinase); FK506 binding protein 12 rapamycin associated protein 1; FRAP, FRAP1, FRAP2; serine/threonine-protein kinase mTOR; dJ576K7.1 (FK506 binding protein 12 rapamycin associated protein 1); FK506

Entrez Gene ID

2475

UniProt ID

P42345

Product Background

Antigen Description

Kinase subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino-acids. 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. Amino-acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. 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-421, which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Phosphorylates MAF1 leading to attenuation of its RNA polymerase III-repressive function. 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.

Pathway

AMPK signaling; Acute myeloid leukemia; Adaptive Immune System; Adipocytokine signaling pathway; Alpha6-Beta4 Integrin Signaling Pathway;

Citations

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Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Customer Reviews

References

Ginsenoside Rg1 Alleviates Podocyte Injury Induced by Hyperlipidemia via Targeting the mTOR/NF-kappa B/NLRP3 Axis

EVIDENCE-BASED COMPLEMENTARY AND ALTERNATIVE MEDICINE

Authors: Wang, Tao; Gao, Yanbin; Yue, Rongchuan; Wang, Xiaolei; Shi, Yimin; Xu, Jiayi; Wu, Bingjie; Li, Yimeng

Abstract

Background. Podocyte injury plays an important role in diabetic nephropathy (DN). The aim of this study was to determine the potential therapeutic effects of the ginsenoside Rg1 on hyperlipidemia-stressed podocytes and elucidate the underlying mechanisms.Methods.In vitroandin vivomodels of DN were established as previously described, and the expression levels of relevant markers were analyzed by Western blotting, real-time Polymerase Chain Reaction (PCR), immunofluorescence, and immunohistochemistry.Results. Ginsenoside Rg1 alleviated pyroptosis in podocytes cultured under hyperlipidemic conditions, as well as in the renal tissues of diabetic rats, and downregulated the mammalian target of rapamycin (mTOR)/NF-kappa B pathway. In addition, Rg1 also inhibited hyperlipidemia-induced NLRP3 inflammasome in the podocytes, which was abrogated by the mTOR activator L-leucine (LEU). The antipyroptotic effects of Rg1 manifested as improved renal function in the DN rats.Conclusion. Ginsenoside Rg1 protects podocytes from hyperlipidemia-induced damage by inhibiting pyroptosis through the mTOR/NF-kappa B/NLRP3 axis, indicating a potential therapeutic function in DN.

Chloride channel 7 protects from redox status impairment-induced renal tubular epithelial cell apoptosis by activating autophagy

LIFE SCIENCES

Authors: Li, Xiang; Du, Yuefeng; Zhang, Linlin; Chen, Xingfa; He, Dalin

Abstract

Aim: Chloride channel 7 (CLC-7), broadly expressed in kidney tissues, affects the lysosome degradation pathway. And redox status impairment contributes to cell apoptosis and activates autophagy flux. This study mainly investigates the role and molecular mechanism of CLC-7 in redox status impairment-induced autophagic flux and apoptosis. Main methods: When NRK52E cells, rat renal tubular epithelial cells, were exposed to H 2 0 2 treatment, apoptosis, autophagy flux, and CLC-7 expression were detected. Further investigation was done to observe the change of apoptosis and autophagy flux in renal cells under overexpression or knocking down of CLC-7. The lysosomes acidity, lysosome enzyme Cathepsin D activity and phosphorylation of Ampk/mTOR were also examined when CLC-7 was overexpressed or knocked down. Key findings: Redox status impairment induced apoptosis and autophagy flux in NRK52E cells and upregulated CLC-7. Overexpression of CLC-7 increased lysosome acidity and Cathepsin D activity. In cells with CLC-7 overexpression, we observed a significant increase of autophagy flux and decline of apoptosis, as well as an apparent increase of p-Ampk and decrease of p-mTOR. On the contrary, cells with knocking down CLC-7 led to opposite results. Significances: CLC-7 is essential to maintain and enhance acidity and enzyme activity in lysosome. Through activating autophagy flux, it exerts survival against renal tubular epithelial cell apoptosis induced by redox status impairment. Its function to modulate Ampk/mTOR pathway is the possible reason why CLC-7 can trigger autophagy flux.