LCB1 Pure 49/LCB1 50ug

Sphingolipid biosynthesis is initiated by condensation of L-serine with palmitoyl coenzyme A, a reaction catalyzed by serine

palmitoyltransferase (SPT). SPT is the rate-determining enzyme in the sphingolipid pathway. This enzyme is a key component for regulating

cellular sphingolipid content. Initially identified in SPT-deficient S. cerevisiae strains, LCB1 and LCB2 homologs have been identified and

characterized in mouse, human, and CHO cell lines. The mammalian LCB1 protein has 35% amino acid identity with yeast LCB1, while the

mammalian LCB2 protein has 43% amino acid identity with yeast LCB2. Both LCB1 and LCB2 are transmembrane proteins containing

protein localization sites, predicting they are membrane-bound enzymes enriched in the endoplasmic reticulum. In mouse tissue, LCB1 and

LCB2 are expressed ubiquitously, with the highest levels detected in kidney and brain. Transfection of SPT-defective CHO mutant strains with

LCB1-expressing plasmid restores both SPT activity and de novo sphingolipid synthesis to wild type levels. Thus, LCB1 may be an essential

component of SPT activity during mammalian sphingolipid biosynthesis.

1.Since applications vary, each investigator should titrate the reagent to obtain optimal results.

2.Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.