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Recombinant Mouse Clusterin Protein, CF

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Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Mouse Clusterin Protein, CF Summary

Details of Functionality
Measured by its ability to induce clustering of Caki‑2 human clear cell carcinoma epithelial cells. Schwochau, G. et al. (1998) Kidney Int. 53:1647.
Source
Mouse myeloma cell line, NS0-derived mouse Clusterin protein
Glu22-Arg226 (beta) & Ser227-Glu448 (alpha), with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Glu22 (beta subunit) & Ser227 (alpha subunit)
Structure / Form
Disulfide-linked heterodimer
Protein/Peptide Type
Recombinant Proteins
Gene
Clu
Purity
>85%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
23.9 kDa (beta subunit) and 26.3 kDa (alpha subunit).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
37 kDa (beta subunit) and 44 kDa (subunit), reducing conditions
Publications
Read Publications using
2747-HS in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>85%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 200 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse Clusterin Protein, CF

  • 40
  • 40, sulfated glycoprotein 2
  • Aging-associated gene 4 protein
  • aging-associated protein 4
  • APOJ
  • apo-J
  • Apolipoprotein J
  • CLI
  • CLIclusterin (complement lysis inhibitor, SP-40
  • CLU
  • Clusterin
  • Complement cytolysis inhibitor
  • complement lysis inhibitor
  • Complement-associated protein SP-40
  • Ku70-binding protein 1
  • KUB1SGP2
  • MGC24903
  • NA1/NA2
  • SGP-2
  • SP-40
  • sulfated glycoprotein 2
  • Testosterone-repressed prostate message 2
  • testosterone-repressed prostate message 2, apolipoprotein J)
  • TRPM-2
  • TRPM-2TRPM2

Background

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).

  1. Carver, J.A. et al. (2003) IUBMB Life 55:661.
  2. Shannan, B. et al. (2006) Cell Death Differ. 13:12.
  3. French, L.E. et al. (1993) J. Cell Biol. 122:1119.
  4. Lee, K.H. et al. (1993) Biochem. Biophys. Res. Commun. 194:1175.
  5. Leskov, K.S. et al. (2003) J. Biol. Chem. 278:11590.
  6. Pankhurst, G.J. et al. (1998) Biochemistry 37:4823.
  7. Burkey, B.F. et al. (1991) J. Lipid. Res. 32:1039.  
  8. de Silva, H.V. et al. (1990) J. Biol. Chem. 265:14292.
  9. Jenne, D.E. et al. (1991) J. Biol. Chem. 266:11030.
  10. Kounnas, M.Z. et al. (1995) J. Biol. Chem. 270:13070.
  11. Pucci, S. et al. (2004) Oncogene 23:2298.
  12. Moretti, R. M. et al. (2007) Cancer Res. 67:10325.
  13. Santilli, G. et al. (2003) J. Biol. Chem. 278:38214.
  14. Trougakos, I.P. et al. (2004) Cancer Res. 64:1834.

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Bioinformatics

Gene Symbol Clu
Uniprot