Cell Signaling Technology

Product Pathways - Translational Control

GβL Antibody #3227

Applications Reactivity Sensitivity MW (kDa) Source
W IP IHC-P H Mk Endogenous 37 Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation  IHC-P=Immunohistochemistry (Paraffin)
Reactivity Key:  H=Human  Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

GβL Antibody detects endogenous levels of total GβL protein.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gln164 of human GβL. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines, using GβL Antibody.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human breast carcinoma, using GβL Antibody in the presence of control peptide (left) or antigen specific peptide (right).

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human lung carcinoma, showing cytoplasmic localization, using GβL Antibody.


IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human transitional epithelial carcinoma of the bladder, using GβL Antibody.

Background

Cell growth is a fundamental biological process whereby cells accumulate mass and increase in size. The mammalian Target of Rapamycin (mTOR) pathway regulates growth by coordinating energy and nutrient signals with growth factor-derived signals (1). mTOR is a large protein kinase with two different complexes. One complex contains mTOR, GβL, and raptor, which is a target of rapamycin. The other complex, insensitive to rapamycin, includes mTOR, GβL, and rictor (1). GβL associates with the kinase domain of mTOR and stimulates mTOR kinase activity (2). A reduction in GβL expression has been shown to decrease in vivo phosphorylation of S6K1 (2).

  1. Sarbassov, D.D. et al. (2004) Curr Biol. 14, 1296-1302.
  2. Kim, D.H. et al. (2003) Mol. Cell 11, 895-904.

Application References

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Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

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