Sphingosine kinase 2 (SPHK2) is an ATP-dependent lipid kinase that is encoded by the SPHK2 gene in humans.{53257} It is composed of an N-terminal domain that contains an ATP binding site and a C-terminal domain that mediates substrate binding and specificity. SPHK2 is localized to the mitochondria, nucleus, and endoplasmic reticulum and is expressed in a wide variety of tissues, including the liver and kidney.{14581} Upon cellular stimulation with EGF, phorbol 12-myristate 13-acetate (PMA; Item No. 10008014), or Fc?RI, SPHK2 is activated and catalyzes phosphorylation of sphingosine to sphingosine-1-phosphate (S1P).{53257,53258} SPHK2 has roles in many physiological and pathological processes, including cancer, inflammation, and neurodegenerative diseases.{53257,14482,53261,53259,53260} Pharmacological inhibition of SPHK2 decreases intracellular S1P levels in U937 cells, but genetic deletion or pharmacological inhibition of SPHK2 in mice increases blood S1P levels, an effect that has not been fully characterized but may be related to reduced S1P clearance in the blood in the absence of SPHK2 activity.{38413} Overexpression of SPHK2 increases intracellular calcium levels and induces apoptosis in NIH3T3 cancer cells and reduces LPS-induced increases in TNF-a and IL-6 levels in isolated human peripheral blood mononuclear cell-derived macrophages in vitro.{14482,53261} SPHK2 activity is increased in postmortem frontal cortex from patients with Alzheimer's disease.{53260} Cayman's Sphingosine Kinase 2 (human, recombinant) protein can be used for Western blot, ELISA, and enzymatic assays.
25 ug
Cayman Chemical
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