SMPD1 Protein, Mouse (sf9, His)

The SMPD1 protein converts sphingomyelin to ceramide through two enzymatic forms, one targeted to endolysosomes and the other released extracellularly. Lysosomal exocytosis becomes a significant source of the secretory form during stress responses. SMPD1 also exports cholesterol from intraendolysosomal membranes and exhibits phospholipase C activities. Its role in stress-induced apoptosis modulation is mediated through ceramide production. SMPD1 Protein, Mouse (sf9, His) is the recombinant mouse-derived SMPD1 protein, expressed by Sf9 insect cells , with C-His labeled tag. The total length of SMPD1 Protein, Mouse (sf9, His) is 626 a.a., with molecular weight of ~63 KDa.

The SMPD1 protein functions by converting sphingomyelin into ceramide through two enzymatic forms derived from alternative trafficking of a single precursor protein. One form is targeted to the endolysosomal compartment, while the other is released extracellularly. However, during stress responses, lysosomal exocytosis may serve as a significant source of the secretory form. Within lysosomes, it carries out the conversion of sphingomyelin to ceramide and plays a crucial role in exporting cholesterol from intraendolysosomal membranes. Additionally, SMPD1 exhibits phospholipase C activities towards 1,2-diacylglycerolphosphocholine and 1,2-diacylglycerolphosphoglycerol. Its involvement in stress-induced apoptosis modulation is mediated through ceramide production.

Mouse

Sf9 insect cells

C-His

Q04519 (M1-L626)

20597  [NCBI]

Approximately 63 kDa.

Greater than 85% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.