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Saposin A Human Recombinant | Scaffolding | Protein - Lipid Nanoparticles System

Amid Biosciences

Saposin A, Human, Recombinant

$ 600.00

Human lysosomes contain four homologous saposins (sphingolipid activator proteins), the saposins A, B, C, and D, which are derived from the prosaposin precursor protein (1, 2).

Saposin A is small, cysteine-rich α-helical glycoprotein that exists in both soluble and lipid-bound states. Saposin A has roles in sphingolipid catabolism and transport and is required for the breakdown of galactosylceramide by β-galactosylceramidase to produce ceramide and galactose (3). 

Saposins are glycosylated in a native state; however, non-glycosylated recombinant saposins produced in E. coli retain their respective activation effects in functional in vitro assays (2). Saposins are used as scaffolding proteins in a versa­tile lipid nanoparticle system to reconstitute membrane proteins in a lipid environment. Saposin-based nanoparticles may have a wide range of potential applications, from structural biology to the therapeutic delivery of protein-based pharmacological agents and vaccines (4).

Recombinant human saposin A is produced in E. coli as an N-terminal His-tag fusion and purified by proprietary chromatography techniques with subsequent removal of the tag trough a site-specific proteolytic cleavage.

Saposin A sequence


Catalog # SAPA-301

Storage buffer: 50 mM Tris-HCl, pH 7.5, 50 mM NaCl, and 50% Glycerol. 
Concentration: 1.0 – 2.0 mg/mL by A280 (E1% 9.3).
Purity: >90% by Coomassie staining 

Storage is recommended at -20°C for longer periods of time. 

International Shipping:  Product requires shipping on ice packs. Please contact for shipment estimates

This product is for laboratory research use only.

Product Manual


Qi, X. Differential membrane interactions of saposins A and C: implications for the functional specificity. J Biol Chem. 2001 Jul 20; 276(29): 27010-7.

Qi, X. et al. Functional human saposins expressed in Escherichia coli. Evidence for binding and activation properties of saposins C with acid beta-glucosidase. J Biol Chem. 1994 Jun 17; 269(24):16746-53.

Popovic, K. et al. Structure of saposin A lipoprotein discs. Proc Natl Acad Sci U S A. 2012 Feb 21; 109(8):2908-12.

Frauenfeld, J. et al. A saposin-lipoprotein nanoparticle system for membrane proteins. Nat Methods. 2016 Apr; 13(4): 345–351.

Lyons, J. et al. Saposin-Lipoprotein Scaffolds for Structure Determination of Membrane Transporters. Methods Enzymol. 2017; 594:85-99.

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