05-1471
Anti-Rictor Antibody, clone 9F1.2
clone 9F1.2, from mouse
别名:
Rictor, AVO3, rapamycin-insensitive companion of mTOR, mAVO3
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关于此项目
UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Conjugate:
unconjugated
Clone:
9F1.2, monoclonal
Application:
immunoprecipitation (IP)
western blot
western blot
Species reactivity:
human, mouse, rat
Citations:
6
Technique(s):
immunoprecipitation (IP): suitable
western blot: suitable
western blot: suitable
Uniprot accession no.:
产品名称
Anti-Rictor Antibody, clone 9F1.2, clone 9F1.2, from mouse
biological source
mouse
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
9F1.2, monoclonal
species reactivity
human, mouse, rat
technique(s)
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG2aκ
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Quality Level
Gene Information
human ... RICTOR(253260)
Analysis Note
Control
HEK293 cell lysate.
Western Blotting Analysis: 1 µg/mL of this antibody detected Rictor on 10 µg of HEK293 cell lysate.
HEK293 cell lysate.
Western Blotting Analysis: 1 µg/mL of this antibody detected Rictor on 10 µg of HEK293 cell lysate.
Evaluated by Western Blotting on 10 mg of HEK293 cell lysate.
Application
Anti-Rictor Antibody, clone 9F1.2 detects level of Rictor & has been published & validated for use in WB & IP.
Immunoprecipitation:
Representative lot data.
1 ug/mL dilution of this antibody immunoprecipitated Rictor from 100 mg of HEK293 lysate.
Representative lot data.
1 ug/mL dilution of this antibody immunoprecipitated Rictor from 100 mg of HEK293 lysate.
Biochem/physiol Actions
This antibody recognizes Rictor.
General description
190 kDa Observed
Rictor, the rapamycin-insensitive complex, is part of the mTORC2 kinase complex which is responsible for phosphorylating the hydrophobic motif kinase of Akt/PKB. This complex also includes mTOR, mSin1 and mLST8/GL. mTORC2 is activated by growth factors and other mitogenic signals.
Immunogen
Recombinant protein corresponding to human Rictor.
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Physical form
Format: Purified
Purified immunoglobulin in buffer containing 0.1 M Tris-Glycine (pH 7.4, 150 mM NaCl) with 0.05% sodium azide.
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存储类别
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Zheng Wang et al.
Neoplasia (New York, N.Y.), 23(11), 1147-1165 (2021-10-28)
Epithelial-mesenchymal transition (EMT) contributes to tumor invasion, metastasis and drug resistance. AKT activation is key in a number of cellular processes. While many positive regulators for either EMT or AKT activation have been reported, few negative regulators are established. Through
Sharon K Kuss-Duerkop et al.
PLoS pathogens, 13(9), e1006635-e1006635 (2017-09-28)
Influenza A virus usurps host signaling factors to regulate its replication. One example is mTOR, a cellular regulator of protein synthesis, growth and motility. While the role of mTORC1 in viral infection has been studied, the mechanisms that induce mTORC1
Sanjit K Dhar et al.
Oncogene, 37(48), 6225-6242 (2018-07-25)
Autophagy is a highly regulated evolutionarily conserved metabolic process induced by stress and energy deprivation. Here, we show that DNA polymerase gamma (Polγ) deficiency activates a selective prosurvival autophagic response via mitochondria-mediated reactive oxygen species (ROS) signaling and the mammalian
Mandy K Losiewicz et al.
Experimental eye research, 197, 108131-108131 (2020-07-06)
The retina is one of the most metabolically active tissues, yet the processes that control retinal metabolism remains poorly understood. The mTOR complex (mTORC) that drives protein and lipid biogenesis and autophagy has been studied extensively in regards to retinal
Mahefatiana Andrianifahanana et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 30(11), 3733-3744 (2016-11-03)
TGF-β plays a central role in the pathogenesis of fibroproliferative disorders. Defining the exact underlying molecular basis is therefore critical for the development of viable therapeutic strategies. Here, we show that expression of the facilitative glucose transporter 1 (GLUT1) is
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