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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Contact

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Product Specifications
Scientific Background

Specifications

NamePurified anti-GβL Antibody, GβL, W18224A
Cat. No.939502
HostRat
RRIDAB_2876768 (BioLegend Cat. No. 939501)AB_2876768 (BioLegend Cat. No. 939502)
IsotypeRat IgG2a, κ
ReactivityHuman, Mouse
ApplicationWB -Quality tested
ClonalityMonoclonal
Clone NumberW18224A
Concentration0.5 mg/mL
TargetGbetaL
ImmunogenFull-length recombinant human GβL protein
PurityThe antibody was purified by affinity chromatography.
FormulationPhosphate-buffered solution, pH 7.2, containing 0.09% sodium azide
StorageThe antibody solution should be stored undiluted between 2°C and 8°C.
Regulatory StatusResearch Use Only

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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