LARS is the critical cytoplasmic enzyme that charges the tRNA for leucine to become L-leucyl-tRNA, or tRNA(Leu). LARS is thus critical for protein biosynthesis and LARS is up regulated, like many proteins, in cancer. LARS is localized in the cytoplasm and regulated via acetylation. Interestingly, recent research demonstrates that LARS and other tRNA synthetases play key roles as amino acid cellular sensors in my cellular signaling pathways such as mTOR which regulate cell size, protein translation, and even autophagy.

~140 kDa observed

KLH-conjugated linear peptide corresponding to human LARS near the C-terminus.

Immunohistochemistry Analysis: A 1:50 dilution from a representative lot detected LARS in human kidney and human liver tissue.

This Anti-LARS Antibody is validated for use in Western Blotting and Immunohistochemistry (Paraffin) for the detection of LARS.

Evaluated by Western Blotting in HUVEC cell lysate.

Western Blotting Analysis: 0.2 µg/mL of this antibody detected LARS in 10 µg of HUVEC cell lysate.

Concentration: Please refer to lot specific datasheet.