Sphingomyelin Synthase 2 (human, recombinant; aa 1-79)

Sphingomyelin synthases (SMSs) are the final enzymes required for the de novo synthesis of sphingomyelin.^1,2 There are three isoforms of sphingomyelin synthase: SMS1, SMS2, and SMSr, which are localized to the Golgi, Golgi and plasma membrane, and endoplasmic reticulum, respectively. All SMSs are composed of six transmembrane domains, with N- and C-terminal cytoplasmic tails. SMS2 also contains four C-terminal palmitoylation sites which are essential to its plasma membrane localization.¹ It is a bifunctional enzyme responsible for the synthesis of both sphingomyelin and ceramide phosphoethanolamine, with sphingomyelin synthesis being its primary function.² SMS2 catalyzes the transfer of a phosphocholine headgroup from phosphatidylcholine to ceramide in the Golgi to produce sphingomyelin. Knockdown of Sgms2, the gene encoding Sms2, decreases M2-like macrophage polarization in vitro and reduces tumor weight and lung metastasis in a 4T1 murine mammary carcinoma model.³ Sgms2 knockdown also inhibits steatosis but increases fibrosis in a mouse model of non-alcoholic steatohepatitis (NASH) induced by a choline-deficient and high-fat diet (CDAHFD).⁴ Cayman’s Sphingomyelin Synthase 2 (human, recombinant; aa 1-79) is a disulfide-linked homodimer. The reduced monomer, composed of SMS2 (amino acids 1-79) fused to mouse IgG1 Fc at its N-terminus, consists of 315 amino acids and has a calculated molecular weight of 35.7 kDa. As a result of glycosylation, the monomer migrates at approximately 45 kDa by SDS-PAGE under reducing conditions.

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1. Yeang, C., Ding, T., Chirico, W.J., et al. Subcellular targeting domains of sphingomyelin synthase 1 and 2. Nutr. Metab. (Lond) 8, 89 (2011).

2. Chen, Y., and Cao, Y. The sphingomyelin synthase family: Proteins, diseases, and inhibitors. Biol. Chem. 398(12), 1319-1325 (2017).

3. Deng, Y., Hu, J.-C., He, S.-H., et al. Sphingomyelin synthase 2 facilitates M2-like macrophage polarization and tumor progression in a mouse model of triple-negative breast cancer. Acta. Pharmacol. Sin. 42(1), 149-159 (2021).

4. Sugimoto, M., Hamada, T., Wakabayasi, M., et al. Sphingomyelin synthase 2 loss suppresses steatosis but exacerbates fibrosis in the liver of mice fed with choline-deficient, L-amino acid-defined, high-fat diet. Biochem. Biophys. Res. Commun. 533(4), 1269-1275 (2020).