Recombinant human LATS2 (480-1088) was expressed by baculovirus in Sf9 insect cells using an N-terminal GST tag.
Catalog No. L02-35G
Catalog No. | Pack Size | Price (USD) | |
---|---|---|---|
L02-35G-20 | 20 ug | $215 | |
L02-35G-50 | 50 ug | $435 | |
L02-35G-BULK | BULK | Contact Us |
Overview:
LATS2 is a serine/threonine protein kinase belonging to the LATS tumor suppressor family (1). The kinase activity and two conserved domains within LATS2 are responsible for the suppression of tumorigenicity and inhibition of cell growth. LATS2 negatively regulates the cell cycle by controlling G1/S and/or G2/M transition. LATS2 interacts with the centrosomal proteins AURORA A and Ajuba and is required for accumulation of γ-tubulin and spindle formation at the onset of mitosis (2). LATS2 also interacts with a negative regulator of p53 and may function in a positive feedback loop with p53 that responds to cytoskeleton damage. LATS2 can also function as a co-repressor of androgen-responsive gene expression.
Gene Aliases:
KPM, FLJ13161
Genbank Number:
References:
1. Li, Y. et al: Lats2, a putative tumor suppressor, inhibits G1/S transition. Oncogene. 2003; 22(28):4398-405.
2. Yabuta, N. et al: Structure, expression, and chromosome mapping of LATS2, a mammalian homologue of the Drosophila tumor suppressor gene lats/warts. Genomics. 2000 63(2):263-70.
Purity:
Sample Purity Data. For specific information on a given lot, see related technical data sheet.
Storage, Stability and Shipping:
Store product at –70oC. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.
Molecular Weight:
~98 kDa
Meistermann Helene et al., A Novel Immuno-Competitive Capture Mass Spectrometry Strategy for Protein-Protein Interaction Profiling Reveals that LATS Kinases Regulate HCV Replication through NS5A Phosphorylation Molecular & Cellular Proteomics July 2014 10.1074/mcp.M113.028977
D Shao et al., A functional interaction between Hippo-YAP signalling and FoxO1 mediates the oxidative stress response. Nature Communications February 2014 10.1038/ncomms4315
Apoptosis/Autophagy, Cancer, Cardiovascular Disease, Cell Cycle
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