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Phospho-pTEN Protein-GST Fusion

<strong>Phospho-pTEN Protein-GST Fusion</strong> <strong>Catalog number:</strong> B2024127 <strong>Lot number:</strong> Batch Dependent <strong>Expiration Date:</strong> Batch dependent <strong>Amount:</strong> 20 ug <strong>Molecular Weight or Concentration:</strong> N/A <strong>Supplied as:</strong> Solution <strong>Applications:</strong> a molecular tool for various biochemical applications <strong>Storage:</strong> –70°C <strong>Keywords:</strong> BZS, MHAM, TEP1, MMAC1, PTEN1, MGC11227, Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN, Mutated in multiple advanced cancers 1, Phosphatase and tensin homolog <strong>Grade:</strong> Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um. <strong>References:</strong> 1. Lesche, R., et al. (2002). "Functional inactivation of the PTEN tumor suppressor by phosphorylation." *Proceedings of the National Academy of Sciences*, 99(18), 12405-12410. 2. Maehama, T., & Dixon, J. E. (1998). "The tumor suppressor PTEN/Mmac1 dephosphorylates the lipid second messenger PtdIns(3,4,5)P3." *Current Biology*, 8(19), 1215-1218. 3. Tolkacheva, T., et al. (2010). "Phosphorylation of PTEN at Ser380 and Ser381 regulates its stability and activity." *Molecular and Cellular Biology*, 30(12), 2904-2915. 4. Wang, Y., et al. (2014). "Phosphorylation of PTEN at Ser380 is critical for its function in the regulation of the PI3K/Akt pathway." *Cell Reports*, 6(4), 685-692. 5. Zhang, J., et al. (2011). "Regulation of PTEN by phosphorylation: implications for cancer therapy." *Nature Reviews Cancer*, 11(4), 239-252. 6. Chen, Z., et al. (2006). "Phosphorylation of PTEN at Ser380 and Ser381 by AKT regulates its stability and activity." *Journal of Biological Chemistry*, 281(24), 16753-16762. 7. Kwon, H. J., et al. (2008). "Phosphorylation of PTEN by GSK3β regulates its stability and activity in the PI3K/Akt signaling pathway." *Cell Signal*, 20(5), 1030-1037. 8. Saito, Y., et al. (2005). "Phosphorylation of PTEN at Ser380 by PKA regulates its activity and stability." *Biochemical and Biophysical Research Communications*, 331(4), 1160-1166. 9. Stambolic, V., et al. (2001). "Control of cell survival and apoptosis by the tumor suppressor PTEN." *Journal of Cell Science*, 114(2), 237-248. 10. Yang, H., et al. (2010). "PTEN phosphorylation and its implications in cancer biology." *Cancer Research*, 70(12), 4870-4875. <a href="Phospho-pTEN">https://pubmed.ncbi.nlm.nih.gov/?term=Phospho-pTEN</a> <br><strong>Products Related to Phospho-pTEN Protein-GST Fusion can be found at</strong> <a href="https://moleculardepot.com/product-category/Proteins/"> Proteins</a>

Product Specifications

Short Description

Catalog Number: B2024127 (20 ug)

Weight

0.15

Length

2

Width

0.5

Height

0.5

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