Anti-Serine Palmitoyltransferase

Sphingolipids play essential roles in various cellular events, including proliferation, differentiation, senescence, apoptosis, and inflammatory responses. 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. Immunohistochemical study revealed widespread distribution of the enzyme with most strong expression in brain and digestive tract. Two subunits, SPT1 and SPT2 at a stoichiometry of 1:1, are involved in the enzymatic activity of SPT. 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.Synonyms: Long Chain Biosynthesis Protein 2 (LCB2), Serine-palmitoyl-CoA transferase 2 (SPT2). Immunogen: Synthetic peptide from the C-terminal region of human SPT2. Formulation: (Request formulation change), Peptide affinity-purified IgG. Storage Buffer: PBS, pH 7.2, with 50% glycerol and 0.02% sodium azide. Host: Rabbit. Applications: IHC and WB. UniProt Accession #: O15270. Origin: Animal/Rabbit.