Purified anti-GβL Antibody, GβL, W18224A,BioLegend,939502
This clone was tested for ICC using HeLa cells fixed with 4% PFA and permeabilized with either Triton X-100 or methanol. Both methods resulted in poor GßL staining.This clone failed to immunoprecipitate GßL from whole cell extracts prepared from HeLa cells.
Host
Rat
Reactivity
Human, Mouse
Application
WB -Quality tested
Platform ID
BAB581977512

BioLegend
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Specifications
Scientific Background
In eukaryotic cells, the serine/threonine kinase mTOR plays a critical role in regulating cell proliferation and metabolism in response to nutrient availability, cellular energy status, growth factors, and stress. mTOR is found as a component of two functionally distinct oligomeric complexes, mTORC1 and mTORC2. mTORC1 coordinates nutrient availability with cell growth and proliferation through phosphorylation of upstream regulators of proliferation and ribosomal biogenesis including 4E-BP1, p70 S6 Kinase 1, and p70 S6 Kinase 2. mTORC2 regulates proliferation and metabolism via phosphorylation of IG-1R, InsR, and Akt, and also plays a role in cytoskeletal architecture and reorganization through modification of Rac1. Both mTORC1 and mTORC2 can drive metabolic adaptation of tumors.GβL, also referred to as mLST8, is a critical structural and scaffolding component of both mTORC1 and mTORC2 signaling complexes. GβL increases mTOR kinase activity by stabilizing the mTOR active site through a direct interaction with the kinase domain. GβL association with mTORC2 is regulated through the action of the TRAF2 E3 ubiquitin ligase, which polyubiquitinates GβL and disrupts its interaction with the mTORC2 assembly factor SIN1. This modification results in a commensurate increase in formation of the mTORC1 complex, which lacks SIN1. Conversely, the deubiquitinating enzyme OTUD7B removes polyubiquintin chains from GβL, thereby promoting assembly of mTORC2.
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