N-terminal His-tagged, recombinant human SHIP2 (truncated form containing SH2 domain and inositol 5-phophatase catalytic domain)

Storage: Store product > -70 ºC. Enzyme is stable for at least 6 months at -70 ºC as undiluted stockSpecificity: SHIP2 selectively removes the phosphate from the 5’ position of the inositol ring of PtdIns(3,4,5)P₃Molecular Weight: 103 kDaSpecific Activity: request Certificate of Analysis (COA)

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.

Publications

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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 5′-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.