Human Prosaposin (PSAP)

Description

Product name: Human Prosaposin (PSAP)

Product description: Recombinant Full-length Human Prosaposin (PSAP) produced in Nicotiana benthamiana by Agrobacterium-mediated transient expression.

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Description

Host species: Nicotiana benthamiana

Molecular weight: 58.1 kDa + Glycosylation

Tag: N-terminal His-tag

Uses: For in vitro research use only. Not for human in vivo or therapeutic use.

Relevance: Prosaposin (PSAP)1 is multidomain glycoprotein that is a precursor for four saposin (A-D) domains which are formed by proteolysis2. The saposin domains are sphingolipid activator proteins which are cofactors for lipid hydrolase enzymes responsible for intralysosomal degradation of sphingolipids3. There are a number of well-documented mutations associated with the PSAP gene that give rise to deficiency in either the full-length PSAP protein (neurovisceral dystrophy) or the individual saposin domains, e.g. Krabbe leukodystroph is caused by saposin-A deficiency, metachromatic leukodystrophy (MLD) by saposin-B deficiency and Gaucher disease which is attributed to saposin-C deficiency4.

Specification
Purity: 98 % as shown by SDS-PAGE

Figure 1: reducing 4-20% SDS-PAGE analysis of 5 µg PSAP.

Biological activity: Active.

Figure 2: neurite outgrowth in SH-SY5Y cells in response to increasing concentration of full-length recombinant human prosaposin or saposin C.

Endotoxin: Not tested.

Storage

Formulation: Lyophilized from PBS pH7.4, 175 mM Trehalose.

Shipping: Recombinant proteins are provided as lyophilized powder which is shipped at ambient temperature.

Stability & Storage: See COA for detailed storage instructions. Lyophilized materials are stable for up to twelve months from the date of receipt at -70℃.

It is recommended that reconstituted protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Reconstitution: A hardcopy of COA with reconstitution instructions is included with the product.

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References
1. https://www.uniprot.org/uniprot/P07602
2. Sandhoff K, Kolter T, Harzer K. Sphingolipid activator proteins. In: Scriver CR, Beaudet AL, Sly WS, Valle D, editors. The Metabolic and molecular bases of inherited diseases. 8th edition. New York: McGraw-Hill. 3371-3388. (2001).
3. Spiegel R, Bach G, Sury V, Mengistu G, Meidan B, Shalev S, Shneor Y, Mandel H, Zeigler M. A mutation in the saposin A coding region of the prosaposin gene in an infant presenting as Krabbe disease: First report of saposin A deficiency in humans. Mol Genet Metab. 16:957–971. (2007).
4. Kuchar L, Ledvinová J, and Harzer K et al. Prosaposin deficiency and saposin B deficiency (activator-deficient metachromatic leukodystrophy): report on two patients detected by analysis of urinary sphingolipids and carrying novel PSAP gene mutations. Am J Med Genet A. 149A(4):613-21. (2009).