N-terminal His-tagged, recombinant human SHIP2 (truncated form containing SH2 domain and inositol 5-phophatase catalytic domain) Storage: Store product > -70 C. Enzyme is stable for at least 6 months at -70 C as undiluted stock Specificity: SHIP2 selectively removes the phosphate from the 5 position of the inositol ring of PtdIns(3,4,5)P3 Molecular Weight: 103 kDa Specific Activity: request Certificate of Analysis (COA)
Product Description: This His-tagged, recombinant human SHIP2 (truncated form containing SH2 domain and inositol 5-phophatase catalytic domain) is tested for activity against PIP3 and is purified from E.coli using Ni-NTA column chromatography. SH2-containing 5 -inositol phosphatase 2 (SHIP2) is a lipid phosphatase which converts PI(3,4,5)P3 to PI(3,4)P2. This negative regulation of insulin signaling has a fundamental impact on insulin resistance. SHIP2 down-regulates insulin signaling and is present at higher levels in diabetes and obesity. Abnormalities in SHIP function are increasingly linked to disease, in particular in the role of SHIP as a negative regulator of cytokine and immune receptor signaling. Featured in Publications: 1.
Drees, B. E., A. Weipert, et al. (2003). Competitive fluorescence polarization assays for the detection of phosphoinositide kinase and phosphatase activity. Comb Chem High Throughput Screen 6(4): 321-30. 2. Brooks, R., G. M. Fuhler, et al. (2010). SHIP1 inhibition increases immunoregulatory capacity and triggers apoptosis of hematopoietic cancer cells. J Immunol 184(7): 3582-9. 3. Fuhler, G. M. B., R, Toms, Iyer, Geno (2012). Therapeutic potential of SHIP1 and SHIP2 inhibition in cancer cells. Molecular Medicine 18: 65-75. 4. Agollah, G. D., et al. (2014). Evidence for SH2 Domain-Containing 5a€-Inositol Phosphatase-2 (SHIP2) Contributing to a Lymphatic Dysfunction. PLoS ONE 9(11): e112548. 5. Proctor, A., et al. (2017). Chemical fixation to arrest phospholipid signaling for chemical cytometry. Journal of Chromatography A 1523(10): 97-106. 6. Willett, R., et al. (2017). TFEB regulates lysosomal positioning by modulating TMEM55B expression and JIP4 recruitment to lysosomes. Nature Communications 8(1): 1580.
Documents: Technical Data Sheet
