Recombinant Human Clusterin Protein, CF

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R&D Systems Recombinant Proteins and Enzymes
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Citations (7)
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Recombinant Human Clusterin Protein, CF Summary

Product Specifications

>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<1.0 EU per 1 μg of the protein by the LAL method.
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.
Mouse myeloma cell line, NS0-derived human Clusterin protein
Asp23-Arg227 (beta) & Ser228-Glu449 (alpha) with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Ser228 ( alpha chain) & Asp23 ( beta chain)
Structure / Form
Disulfide-linked heterodimer
Predicted Molecular Mass
26.7 kDa ( alpha chain) and 24.2 kDa ( beta chain)
40 kDa and 39 kDa, under reducing conditions

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Carrier Free

What does CF mean?

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.

What formulation is right for me?

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.


Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 250 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.
  • 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.
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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). Human Clusterin is synthesized as a precursor that contains two coiled coil domains, three nuclear localization signals (NLS), and one heparin binding domain (4-6). 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 human Clusterin shares 77% amino acid sequence identity with mouse and rat Clusterin. 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. Kirszbaum, L. et al. (1989) EMBO J. 8:711.
  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.
Entrez Gene IDs
1191 (Human); 12759 (Mouse)
Alternate Names
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

Citations for Recombinant Human 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.

7 Citations: Showing 1 - 7
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  1. Clusterin exacerbates interleukin-1beta-induced inflammation via suppressing PI3K/Akt pathway in human fibroblast-like synoviocytes of knee osteoarthritis
    Authors: T Ungsudecha, S Honsawek, J Jittikoon, W Udomsinpra
    Oncogene, 2022;12(1):9963.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. GAD1 Upregulation Programs Aggressive Features of Cancer Cell Metabolism in the Brain Metastatic Microenvironment
    Authors: PM Schnepp, DD Lee, IH Guldner, TK O'Tighearn, EN Howe, B Palakurthi, KE Eckert, TA Toni, BL Ashfeld, S Zhang
    Cancer Res., 2017;0(0):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Protective effect of clusterin on rod photoreceptor in rat model of retinitis pigmentosa
    Authors: A Vargas, HS Kim, E Baral, WQ Yu, CM Craft, EJ Lee
    PLoS ONE, 2017;12(8):e0182389.
    Species: Rat
    Sample Types: In Vivo
    Applications: In Vivo
  4. Clusterin in the protein corona plays a key role in the stealth effect of nanoparticles against phagocytes
    Authors: Michihiko Aoyama
    Biochem. Biophys. Res. Commun, 2016;0(0):.
    Applications: Bioassay
  5. 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;10(9):e0138958.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  6. Clusterin and complement activation in exfoliation glaucoma.
    Authors: Doudevski, Ivo, Rostagno, Agueda, Cowman, Mary, Liebmann, Jeffrey, Ritch, Robert, Ghiso, Jorge
    Invest Ophthalmol Vis Sci, 2014;55(4):2491-9.
    Species: Human
    Sample Types: Protein
    Applications: Western Blot
  7. Identification of novel substrates for the serine protease HTRA1 in the human RPE secretome.
    Authors: An E, Sen S, Park SK, Gordish-Dressman H, Hathout Y
    Invest. Ophthalmol. Vis. Sci., 2010;51(7):3379-86.
    Species: Human
    Sample Types: Protein
    Applications: Enzyme Assay Substrate


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