Recombinant Human PSP Protein, CF
Recombinant Human PSP Protein, CF Summary
Product Specifications
Leu21-Ile249, with a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
5498-PS
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 500 μg/mL in sterile PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Reconstitution Calculator
Background: PSP
Parotid secretory protein (PSP; also short palate, lung, nasal epithelium carcinoma-associated protein 2 or SPLUNC2 and C20orf70) is a 36 ‑ 40 kDa secreted glycoprotein and member of the Bactericidal permeability-increasing (BPI)/Lipopolysaccharide-binding protein (LBP)/PLUNC superfamily and PLUNC family of proteins (1). Human PSP is synthesized as a 249 amino acid (aa) precursor that contains an 18 aa signal sequence and a 231 aa mature chain. The mature chain contains one BPI/LBS/PLUNC domain (aa 62 ‑ 220) and two potential sites for N-linked glycosylation. Mature human PSP is 31% and 26% aa identical to mature mouse and rat PSP, respectively. Human PSP is expressed in the parotid and submandibular glands in ductal epithelial cells and acinar cells (1 - 2). PSP has been shown to exhibit bacteristatic and bactericidal effects on Pseudomonas aerginosa (1). In addition, PSP‑derived peptides inhibit the binding of endotoxin to LBP and inhibit the endotoxin‑stimulated secretion of tumor necrosis factor alpha from macrophages (1, 3). These findings suggest that PSP peptides can serve as templates for the design of novel anti-inflammatory peptides (3). One study showed that peptide GL‑13 induced bacterial matting, suggesting passive agglutination of bacteria (4). GL-13 was shown to agglutinate Gram negative bacteria P. aerginosa and Aggregatibacter (Actinobacillus) actinomycetemcomitans, Gram positive Streptococcus gordonii and uncoated sheep erythrocytes (4). The agglutination leads to increased clearance by host phagocytic cells.
- Geetha, C. et al. (2003) Biochem. Soc. Trans. 31:815.
- Bingle, C.D. and S.-U. Gorr (2004) Int. J. Biochem. Cell Biol. 36:2144.
- Geetha, C. et al. (2005) J. Dent. Res. 84:149.
- Gorr, S.-U. et al. (2008) Peptides 29:2118.
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