Saposin D, Human, Recombinant

Saposin D (SAP-D) is a small, heat-stable lysosomal glycoprotein derived from the prosaposin precursor protein via site-specific proteolytic cleavage. It functions as an indispensable non-enzymatic cofactor required for the lysosomal breakdown of ceramides into free fatty acids and sphingosine by acid ceramidase (ASAH1). Deficiencies in functional Saposin D or its cognate enzyme lead to severe ceramide accumulation, causing lysosomal storage disorders such as Farber lipogranulomatosis. While native saposins feature complex glycosylation patterns, non-glycosylated recombinant saposins expressed in bacterial systems retain full biological activation properties in functional in vitro biochemical and lipid reconstitution assays.

Key Research & Assay Applications

• Ceramide Catabolism & Enzymology: Functions as a vital cofactor for reconstituting in vitro acid ceramidase enzyme kinetics and lipid-cleaving mechanics.
• Lipidomics & Membrane Biophysics: Used in downstream structural biochemistry profiling to study protein-lipid bilayer interactions and membrane permeabilization.
• Therapeutic & Chaperone Screening: High-value target component for screening small molecule chaperones, enzyme replacement therapies (ERT), or drug designs targeting Farber disease pathways.

Product Features & Specifications

• Expression System: Engineered and produced in an optimized Escherichia coli (E. coli) bacterial expression platform.
• Tag Status: Expressed as an N-terminal His-tag fusion and purified using proprietary chromatography steps, followed by site-specific proteolytic cleavage to yield a completely tag-free final protein.
• High Purity: Formulated to >90% purity as verified by Coomassie blue staining on SDS-PAGE.
• Storage Buffer: Supplied at a concentration of 0.5 – 2.0 mg/mL in 10 mM Tris-HCl, pH 7.5, 100 mM NaCl, and 50% Glycerol for premium structural stability.

Catalog Number: SAPD-301-1 | This product is intended for laboratory research use only (RUO). Product requires shipping on ice packs.