Serine Palmitoyltransferase Polyclonal Antibody

Sphingolipids play essential roles in various cellular events, including proliferation, differentiation, senescence, apoptosis, and inflammatory responses.¹ Serine palmitoyltransferase (SPT) is the initial and rate-limiting enzyme in the de novo sphingolipid biosynthesis, and thus regulates the level of sphingolipids in cells.² Immunohistochemical study revealed widespread distribution of the enzyme with most strong expression in brain and digestive tract.³ Two subunits, SPT1 and SPT2 at a stoichiometry of 1:1, are involved in the enzymatic activity of SPT.⁴ Cayman Chemical’s SPT2 Polyclonal Antibody recognizes SPT2, the long chain subunit of the enzyme. The antibody stains mainly cell nuclei and occasionally both cell nuclei and cytoplasm in formalin-fixed, paraffin-embedded rat brain tissue. The nuclear localization of SPT2 may suggest that SPT2 associates with another nuclear protein or is modified and transported to the nucleus.²

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1. Mathias, S., Peña, L.A., and Kolesnick, R.N. Signal transduction of stress via ceramide. Biochem. J. 335, 465-480 (1998).

2. Carton, J.M., Uhlinger, D.J., Batheja, A.D., et al. Enhanced serine palmitoyltransferase expression in proliferating fiboblasts, transformed cell lines, and human tumors. J. Histochem. Cytochem. 51(6), 715-726 (2003).

3. Batheja, A.D., Uhlinger, D.J., Carton, J.M., et al. Characterization of serine palmitoyltransferase in normal human tissues. J. Histochem. Cytochem. 51(5), 687-696 (2003).

4. Hanada, K., Hara, T., and Nishijima, M. Purification of the serine palmitoyltransferase complex responsible for sphingoid base synthesis by using affinity peptide chromatography techniques. The Journal of Biological Chemisty 275(12), 8409-8415 (2000).