Anti-Sphingosine Kinase 2 (Thr-578), Phosphospecific Antibody

Sphingolipids are metabolized into bioactive products that include ceramide, sphingosine, and sphingosine-1-phosphate (S1P) . Sphingosine Kinase (SK) catalyzes the phosphorylation of the lipid sphingosine, creating S1P. S1P subsequently signals through cell surface G protein-coupled receptors, as well as intracellularly, to modulate cell proliferation, survival, motility and differentiation. Two isoforms of SK have been identified, SK1 and SK2. The mRNA for both of these isoforms is widely expressed with SK1 expression highest in brain, heart, kidney, thymus, spleen and lung, while SK2 is highest in kidney and liver. SKs can be activated through growth factor, G protein-coupled, and immunoglobulin receptor signalling. Regulation of SK1 and SK2 activity may occur through phosphorylation. SK1 is phosphorylated at Ser-225 by ERK leading to increased activity and translocation to the plasma membrane. SK2 is phosphorylated in response to EGF, PKC activators, and phorbol esters. ERK1 can phosphorylate both Ser-351 and Thr-578, and non-phosphorylatable mutants of these sites suppress ERK1-mediated chemotaxis.

Our Sphingosine Kinase 2 (Thr-578) rabbit polyclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects human, mouse, and rat Sphingosine Kinase 2 (Thr-578) and is antigen affinity purified. It is great for use in WB.

Phospho-SK2 (Thr-578) synthetic peptide (coupled to KLH) corresponding to amino acid residues surrounding Thr-578 in human SK2. This peptide sequence is highly conserved in rat and mouse SK2 proteins, and is not well conserved in SK1.

For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.

The antibody detects 70 kDa* proteins corresponding to the molecular mass of SK2 on SDS-PAGE immunoblots of human recombinant SK2 and endogenous SK2 in human HeLa cells treated with calyculin A. This reactivity is not observed after lambda phosphatase treatment.