Recombinant Mouse Clusterin Protein, CF Summary
Product Specifications
Glu22-Arg226 (beta) & Ser227-Glu448 (alpha), 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.
2747-HS
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 200 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: Clusterin
Clusterin, also known as Apolipoprotein J, Sulfated Glycoprotein 2 (SGP-2), TRPM-2, and SP-40,40, is a secreted multifunctional protein that was named for its ability to induce cellular clustering. It binds a wide range of molecules and may function as a chaperone of misfolded extracellular proteins. It also participates in the control of cell proliferation, apoptosis, and carcinogenesis (1, 2). Clusterin is predominantly expressed in adult testis, ovary, adrenal gland, liver, heart, and brain and in many epithelial tissues during embryonic development (3). Mouse Clusterin is synthesized as a precursor that contains two coiled coil domains, two nuclear localization signals (NLS), and one heparin binding domain (3-6). Intracellular cleavages of the precursor remove the signal peptide and generate comparably sized alpha and beta chains which are secreted as an 80 kDa N-glycosylated disulfide-linked heterodimer (7, 8). Mature mouse Clusterin shares 77% and 93% amino acid sequence identity with human and rat Clusterin, respectively. High μg/mL concentrations of Clusterin circulate predominantly as a component of high density lipoprotein particles, and these are internalized and degraded through interactions with LRP-2/Megalin (9, 10). In human, an alternately spliced 50 kDa isoform of Clusterin (nCLU) lacks the signal peptide and remains intracellular (5, 11). This molecule is neither glycosylated nor cleaved into alpha and beta chains (11). In the cytoplasm, nCLU destabilizes the actin cytoskeleton and inhibits NF kappa B activation (12, 13). Cellular exposure to ionizing radiation promotes the translocation of nCLU to the nucleus where it interacts with Ku70 and promotes apoptosis (5, 11). This function contrasts with the cytoprotective effect of secreted Clusterin (14). During colon cancer tumor progression there is a down-regulation of the intracellular form and an up-regulation of the glycosylated secreted form (11).
- Carver, J.A. et al. (2003) IUBMB Life 55:661.
- Shannan, B. et al. (2006) Cell Death Differ. 13:12.
- French, L.E. et al. (1993) J. Cell Biol. 122:1119.
- Lee, K.H. et al. (1993) Biochem. Biophys. Res. Commun. 194:1175.
- Leskov, K.S. et al. (2003) J. Biol. Chem. 278:11590.
- Pankhurst, G.J. et al. (1998) Biochemistry 37:4823.
- Burkey, B.F. et al. (1991) J. Lipid. Res. 32:1039.
- de Silva, H.V. et al. (1990) J. Biol. Chem. 265:14292.
- Jenne, D.E. et al. (1991) J. Biol. Chem. 266:11030.
- Kounnas, M.Z. et al. (1995) J. Biol. Chem. 270:13070.
- Pucci, S. et al. (2004) Oncogene 23:2298.
- Moretti, R. M. et al. (2007) Cancer Res. 67:10325.
- Santilli, G. et al. (2003) J. Biol. Chem. 278:38214.
- Trougakos, I.P. et al. (2004) Cancer Res. 64:1834.
Citations for Recombinant Mouse Clusterin Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Clusterin deficiency induces lipid accumulation and tissue damage in kidney
Authors: JY Heo, JE Kim, Y Dan, YW Kim, JY Kim, KH Cho, YK Bae, SS Im, KH Liu, IH Song, JR Kim, IK Lee, SY Park
J. Endocrinol., 2018-03-21;0(0):.
Species: Rat
Sample Types: Whole Cells
Applications: Bioassay -
Clusterin signals via ApoER2/VLDLR and induces meiosis of male germ cells
Authors: MA Riaz, A Stammler, M Borgers, L Konrad
Am J Transl Res, 2017-03-15;9(3):1266-1276.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Clusterin Seals the Ocular Surface Barrier in Mouse Dry Eye.
Authors: Bauskar A, Mack W, Mauris J, Argueso P, Heur M, Nagel B, Kolar G, Gleave M, Nakamura T, Kinoshita S, Moradian-Oldak J, Panjwani N, Pflugfelder S, Wilson M, Fini M, Jeong S
PLoS ONE, 2015-09-24;10(9):e0138958.
Species: Mouse
Sample Types: In Vivo
Applications: In Vivo
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