Recombinant Human Pentraxin 3/TSG-14 His-tag Protein, CF
Recombinant Human Pentraxin 3/TSG-14 His-tag Protein, CF Summary
Product Specifications
Glu18-Ser381, with a C-terminal 6-His tag
Analysis
Product Datasheets
10292-TS
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.
10292-TS
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Reconstitution | Reconstitute at 500 μg/mL in 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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Scientific Data
When Human C1q is immobilized at 5 μg/mL (100 μL/well), Recombinant Human Pentraxin 3/TSG-14 His-tag (Catalog # 10292-TS) binds with an ED50 of 0.5-4 μg/mL.
2 μg/lane of Recombinant Human Pentraxin 3/TSG-14 His-tag (Catalog # 10292-TS) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 38-55 kDa under reducing condition.
Background: Pentraxin 3/TSG-14
Pentraxin 3 (PTX3), TSG-14, was initially identified as a TNF-alpha or IL-1 beta inducible gene (1-3). It belongs to the pentraxin family, which was named originally for the homo-pentameric structure formed by its members (4). The pentraxin family is divided into two subfamilies: the “short” and the “long” pentraxins with approximate molecular weights of 25 kDa and 50 kDa, respectively. TSG-14 is a member of the long pentraxin subfamily, which also includes the Xenopus laevis XL-PXN1, the guinea pig apexin/p50, the rat neuronal pentraxin I (NPI) and NPR, the human neuronal pentraxin II (NPTX2) and the human neuronal activity-related pentraxin (5). Mature secreted TSG-14 contains a pentaxin-like domain at its carboxy-terminus that shares 23-28% amino acid (aa) sequence similarity to C-reactive protein (CRP) and serum amyloid P component (SAP), which belongs to the short pentraxin subfamily. However, the N-terminal sequence of TSG-14 does not share aa sequence homology with any of the “short” pentaxins (3). Unlike CRP and SAP, which forms pentamers only, TSG-14 forms both pentameric and higher ordered oligomers (5). Similarly to CRP and SAP, TSG-14 binds to the complement cascade component C1q (6). However, TSG-14 does not bind to phosphoethanolamine, phosphocholine, or high pyruvate agarose, which are known ligands for CRP and SAP. TSG-14 is a marker of the acute phase response and is highly expressed in advanced atherosclerotic plaques (12). While CRP and SAP are primarily produced in the liver, TSG-14 expression is strongly upregulated by TNF-alpha, IL-1 beta, and bacterial LPS in peripheral fibroblasts, endothelial cells, and macrophages (7). At the amino acid level, human and mouse TSG-14 share 88% aa sequence homology (8). TSG-14 concentration is elevated in the joint fluid of patients with rheumatoid arthritis (RA), indicating that TSG-14 may be a potential mediator of immune response (9). TSG-14 may also function in the regulation of the uptake and clearance of apoptotic cells by dendritic cells (10). In vivo study showed that TSG-14 transgenic mice are more resistant to sepsis and endotoxemia compared to wild type during the inflammatory injury (11). Increased expression of TSG-14 may enhance the immune response to protect the host from infection.
- Lee, T.H. et al. (1990) Mol. Cell. Biol. 10:1982.
- Breviario, F. et al. (1992) J. Biol. Chem. 267:22190.
- Lee, G.W. et al. (1993) J. Immunol. 150:1804.
- Osmand, A.P. et al. (1977) Proc. Natl. Acad. Sci. USA 74:739.
- Goodman A.R. et al. (1996) Cytokine & Growth Factor Reviews 7:191.
- Bottazzi, B. et al. (1997) J. Biol. Chem. 272:32817.
- Introna, M. et al. (1996) Blood 87:1862.
- Altmeyer, A. et al. (1995) J. Biol. Chem. 270:25584.
- Luchetti, M.M. et al. (2000) Clin. Exp. Immunol. 119:196.
- Rovere, P. et al. (2000) Blood 96:4300.
- Dias, A.A.M. et al. (2001) J. Leukocyte Biol. 69:928.
- Rolph, M.S. et al. (2002) Arterioscler. Throm. Vasc. Biol. 22:e10-4.
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