- Species ReactivityHuman
- SpecificityDetects human Clusterin in direct ELISAs and Western blots. In direct ELISAs and Western blots, approximately 40% cross-reactivity with recombinant mouse Clusterin is observed and less than 5% cross-reactivity with recombinant rat Clusterin is observed.
- SourcePolyclonal Goat IgG
- PurificationAntigen Affinity-purified
- ImmunogenMouse myeloma cell line NS0-derived recombinant human Clusterin isoform 1 (R&D Systems, Catalog # 2937-HS)
Asp75-Glu501
Accession # NP_001822 - FormulationLyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
- LabelUnconjugated
- Western Blot1 µg/mLSee below
- Immunohistochemistry5-15 µg/mLSee below
- Immunoprecipitation25 µg/mLConditioned cell culture medium spiked with Recombinant Human Clusterin (Catalog # 2937‑HS), see our available Western blot detection antibodies
- ReconstitutionReconstitute at 0.2 mg/mL in sterile PBS.
- ShippingThe product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
- Stability & StorageUse 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.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
- 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.
- Kirszbaum, L. et al. (1989) EMBO J. 8:711.
- 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.
- 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
Background:
Clusterin, also known as Apolipoprotein J, Sulfated Glycoprotein 2 (SGP-2), TRPM-2, and SP-40,40, is a secreted multi-functional 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 sizedalphaandbetachains 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 intoalphaandbetachains (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 downregulation of the intracellular form and an upregulation of the glycosylated secreted form (11).
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