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

Phosphatidylcholine:ceramide Cholinephosphotransferase 2|SMS2

Sphingomyelin synthases (SMSs) are the final enzymes required for the de novo synthesis of sphingomyelin.{67837,67836} 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.{67837} It is a bifunctional enzyme responsible for the synthesis of both sphingomyelin and ceramide phosphoethanolamine, with sphingomyelin synthesis being its primary function.{67836} 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.{67838} 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).{67839} 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.

-80

-80

Lyophilized from sterile PBS, pH 7.4

365

≥95% estimated by SDS-PAGE