Saposin A, Human, Recombinant | Amid Biosciences
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 chromatographic techniques.
Catalog # SAPA-301
Storage buffer: 50 mM Tris-HCl, pH 7.5, 50 mM NaCl, and 50% Glycerol.
Concentration: 1.0 mg/mL by A280
Purity: >90% by Coomassie staining
Storage is recommended at -20°C for longer periods of time.
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This product is for laboratory research use only.
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.
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.