| Reactivity | HuSpecies Glossary |
| Applications | WB, IHC, IP |
| Clonality | Polyclonal |
| Host | Goat |
| Conjugate | Unconjugated |
| Concentration | LYOPH |
| Immunogen | Mouse myeloma cell line NS0-derived recombinant human Clusterin isoform 1 Asp75-Glu501 Accession # NP_001822 |
| Specificity | Detects 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. |
| Source | N/A |
| Isotype | IgG |
| Clonality | Polyclonal |
| Host | Goat |
| Gene | CLU |
| Purity Statement | Antigen Affinity-purified |
| Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
| Dilutions |
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| Publications |
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| Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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| Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS. |
| Preservative | No Preservative |
| Concentration | LYOPH |
| Reconstitution Instructions | Reconstitute at 0.2 mg/mL in sterile PBS. |
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 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 downregulation of the intracellular form and an upregulation of the glycosylated secreted form (11).
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Secondary Antibodies |
Isotype Controls |
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![Extracellular clusterin interacts with alpha ‐synuclein preformed fibrils (pffs). (a) Medium from primary astrocytes treated with alpha ‐synuclein pffs for 16 hr, or with monomeric alpha ‐synuclein (m), were subjected to immunoblotting using clusterin antibody. Ponceau‐S staining was used as a loading control. (b) Quantification of clusterin is normalized to GAPDH protein of cell lysates. Data are from eight independent experiments and are expressed as the mean ± SD. Data were analyzed using unpaired t test; **p = .0028. (c) alpha ‐Synuclein pffs isolated by centrifugation from total medium of primary astrocytes treated with alpha ‐synuclein pffs, or monomeric alpha ‐synuclein (M), for 16 hr were subjected to immunoblotting using clusterin and alpha ‐synuclein antibodies. Asterisk in the alpha ‐synuclein immunoblot indicates clusterin bands still present after Clusterin antibody stripping. (d) Clusterin immunoprecipitated from the medium of primary astrocytes treated with alpha ‐synuclein pffs for 16 hr was subjected to immunoblotting using an alpha ‐synuclein antibody. (e) Quantification of clusterin— alpha ‐synuclein pffs interaction has been obtained by normalization of alpha ‐synuclein pffs bound to clusterin for alpha ‐synuclein pffs bound to protein‐G beads. Data are representative of three independent experiments and are expressed as the mean ± SD. Data were analyzed using one‐sample t test; *p = .0493. (f) Z‐stack frames of primary astrocytes treated with alpha ‐synuclein pffs for 16 hr and stained for alpha ‐synuclein (purple), clusterin (green), cadherin (red), and nuclei with DAPI (blue). Scale bar 10 μm. (g) Maximum intensity Z‐projection confocal images of primary astrocytes treated with alpha ‐synuclein pffs for 16 hr and stained for alpha ‐synuclein (purple), clusterin (red), Early Endosome Antigen 1 (EEA1) (green) and nuclei with DAPI (blue). Scale bar 10 μm. Individual points of the graphs represent each single experiment [Color figure can be viewed at wileyonlinelibrary.com] Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33045109), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/af2937_human-clusterin-affinity-purified-polyclonal-ab-41202412401226.jpg "Extracellular clusterin interacts with alpha ‐synuclein preformed fibrils (pffs). (a) Medium from primary astrocytes treated with alpha ‐synuclein pffs for 16 hr, or with monomeric alpha ‐synuclein (m), were subjected to immunoblotting using clusterin antibody. Ponceau‐S staining was used as a loading control. (b) Quantification of clusterin is normalized to GAPDH protein of cell lysates. Data are from eight independent experiments and are expressed as the mean ± SD. Data were analyzed using unpaired t test; **p = .0028. (c) alpha ‐Synuclein pffs isolated by centrifugation from total medium of primary astrocytes treated with alpha ‐synuclein pffs, or monomeric alpha ‐synuclein (M), for 16 hr were subjected to immunoblotting using clusterin and alpha ‐synuclein antibodies. Asterisk in the alpha ‐synuclein immunoblot indicates clusterin bands still present after Clusterin antibody stripping. (d) Clusterin immunoprecipitated from the medium of primary astrocytes treated with alpha ‐synuclein pffs for 16 hr was subjected to immunoblotting using an alpha ‐synuclein antibody. (e) Quantification of clusterin— alpha ‐synuclein pffs interaction has been obtained by normalization of alpha ‐synuclein pffs bound to clusterin for alpha ‐synuclein pffs bound to protein‐G beads. Data are representative of three independent experiments and are expressed as the mean ± SD. Data were analyzed using one‐sample t test; *p = .0493. (f) Z‐stack frames of primary astrocytes treated with alpha ‐synuclein pffs for 16 hr and stained for alpha ‐synuclein (purple), clusterin (green), cadherin (red), and nuclei with DAPI (blue). Scale bar 10 μm. (g) Maximum intensity Z‐projection confocal images of primary astrocytes treated with alpha ‐synuclein pffs for 16 hr and stained for alpha ‐synuclein (purple), clusterin (red), Early Endosome Antigen 1 (EEA1) (green) and nuclei with DAPI (blue). Scale bar 10 μm. Individual points of the graphs represent each single experiment [Color figure can be viewed at wileyonlinelibrary.com] Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33045109), licensed under a CC-BY license. Not internally tested by R&D Systems.")
![Extracellular clusterin interacts with alpha ‐synuclein preformed fibrils (pffs). (a) Medium from primary astrocytes treated with alpha ‐synuclein pffs for 16 hr, or with monomeric alpha ‐synuclein (m), were subjected to immunoblotting using clusterin antibody. Ponceau‐S staining was used as a loading control. (b) Quantification of clusterin is normalized to GAPDH protein of cell lysates. Data are from eight independent experiments and are expressed as the mean ± SD. Data were analyzed using unpaired t test; **p = .0028. (c) alpha ‐Synuclein pffs isolated by centrifugation from total medium of primary astrocytes treated with alpha ‐synuclein pffs, or monomeric alpha ‐synuclein (M), for 16 hr were subjected to immunoblotting using clusterin and alpha ‐synuclein antibodies. Asterisk in the alpha ‐synuclein immunoblot indicates clusterin bands still present after Clusterin antibody stripping. (d) Clusterin immunoprecipitated from the medium of primary astrocytes treated with alpha ‐synuclein pffs for 16 hr was subjected to immunoblotting using an alpha ‐synuclein antibody. (e) Quantification of clusterin— alpha ‐synuclein pffs interaction has been obtained by normalization of alpha ‐synuclein pffs bound to clusterin for alpha ‐synuclein pffs bound to protein‐G beads. Data are representative of three independent experiments and are expressed as the mean ± SD. Data were analyzed using one‐sample t test; *p = .0493. (f) Z‐stack frames of primary astrocytes treated with alpha ‐synuclein pffs for 16 hr and stained for alpha ‐synuclein (purple), clusterin (green), cadherin (red), and nuclei with DAPI (blue). Scale bar 10 μm. (g) Maximum intensity Z‐projection confocal images of primary astrocytes treated with alpha ‐synuclein pffs for 16 hr and stained for alpha ‐synuclein (purple), clusterin (red), Early Endosome Antigen 1 (EEA1) (green) and nuclei with DAPI (blue). Scale bar 10 μm. Individual points of the graphs represent each single experiment [Color figure can be viewed at wileyonlinelibrary.com] Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33045109), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/af2937_human-clusterin-affinity-purified-polyclonal-ab-41202412401245.jpg "Extracellular clusterin interacts with alpha ‐synuclein preformed fibrils (pffs). (a) Medium from primary astrocytes treated with alpha ‐synuclein pffs for 16 hr, or with monomeric alpha ‐synuclein (m), were subjected to immunoblotting using clusterin antibody. Ponceau‐S staining was used as a loading control. (b) Quantification of clusterin is normalized to GAPDH protein of cell lysates. Data are from eight independent experiments and are expressed as the mean ± SD. Data were analyzed using unpaired t test; **p = .0028. (c) alpha ‐Synuclein pffs isolated by centrifugation from total medium of primary astrocytes treated with alpha ‐synuclein pffs, or monomeric alpha ‐synuclein (M), for 16 hr were subjected to immunoblotting using clusterin and alpha ‐synuclein antibodies. Asterisk in the alpha ‐synuclein immunoblot indicates clusterin bands still present after Clusterin antibody stripping. (d) Clusterin immunoprecipitated from the medium of primary astrocytes treated with alpha ‐synuclein pffs for 16 hr was subjected to immunoblotting using an alpha ‐synuclein antibody. (e) Quantification of clusterin— alpha ‐synuclein pffs interaction has been obtained by normalization of alpha ‐synuclein pffs bound to clusterin for alpha ‐synuclein pffs bound to protein‐G beads. Data are representative of three independent experiments and are expressed as the mean ± SD. Data were analyzed using one‐sample t test; *p = .0493. (f) Z‐stack frames of primary astrocytes treated with alpha ‐synuclein pffs for 16 hr and stained for alpha ‐synuclein (purple), clusterin (green), cadherin (red), and nuclei with DAPI (blue). Scale bar 10 μm. (g) Maximum intensity Z‐projection confocal images of primary astrocytes treated with alpha ‐synuclein pffs for 16 hr and stained for alpha ‐synuclein (purple), clusterin (red), Early Endosome Antigen 1 (EEA1) (green) and nuclei with DAPI (blue). Scale bar 10 μm. Individual points of the graphs represent each single experiment [Color figure can be viewed at wileyonlinelibrary.com] Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33045109), licensed under a CC-BY license. Not internally tested by R&D Systems.")
![Extracellular clusterin interacts with alpha ‐synuclein preformed fibrils (pffs). (a) Medium from primary astrocytes treated with alpha ‐synuclein pffs for 16 hr, or with monomeric alpha ‐synuclein (m), were subjected to immunoblotting using clusterin antibody. Ponceau‐S staining was used as a loading control. (b) Quantification of clusterin is normalized to GAPDH protein of cell lysates. Data are from eight independent experiments and are expressed as the mean ± SD. Data were analyzed using unpaired t test; **p = .0028. (c) alpha ‐Synuclein pffs isolated by centrifugation from total medium of primary astrocytes treated with alpha ‐synuclein pffs, or monomeric alpha ‐synuclein (M), for 16 hr were subjected to immunoblotting using clusterin and alpha ‐synuclein antibodies. Asterisk in the alpha ‐synuclein immunoblot indicates clusterin bands still present after Clusterin antibody stripping. (d) Clusterin immunoprecipitated from the medium of primary astrocytes treated with alpha ‐synuclein pffs for 16 hr was subjected to immunoblotting using an alpha ‐synuclein antibody. (e) Quantification of clusterin— alpha ‐synuclein pffs interaction has been obtained by normalization of alpha ‐synuclein pffs bound to clusterin for alpha ‐synuclein pffs bound to protein‐G beads. Data are representative of three independent experiments and are expressed as the mean ± SD. Data were analyzed using one‐sample t test; *p = .0493. (f) Z‐stack frames of primary astrocytes treated with alpha ‐synuclein pffs for 16 hr and stained for alpha ‐synuclein (purple), clusterin (green), cadherin (red), and nuclei with DAPI (blue). Scale bar 10 μm. (g) Maximum intensity Z‐projection confocal images of primary astrocytes treated with alpha ‐synuclein pffs for 16 hr and stained for alpha ‐synuclein (purple), clusterin (red), Early Endosome Antigen 1 (EEA1) (green) and nuclei with DAPI (blue). Scale bar 10 μm. Individual points of the graphs represent each single experiment [Color figure can be viewed at wileyonlinelibrary.com] Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33045109), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/af2937_human-clusterin-affinity-purified-polyclonal-ab-41202412402530.jpg "Extracellular clusterin interacts with alpha ‐synuclein preformed fibrils (pffs). (a) Medium from primary astrocytes treated with alpha ‐synuclein pffs for 16 hr, or with monomeric alpha ‐synuclein (m), were subjected to immunoblotting using clusterin antibody. Ponceau‐S staining was used as a loading control. (b) Quantification of clusterin is normalized to GAPDH protein of cell lysates. Data are from eight independent experiments and are expressed as the mean ± SD. Data were analyzed using unpaired t test; **p = .0028. (c) alpha ‐Synuclein pffs isolated by centrifugation from total medium of primary astrocytes treated with alpha ‐synuclein pffs, or monomeric alpha ‐synuclein (M), for 16 hr were subjected to immunoblotting using clusterin and alpha ‐synuclein antibodies. Asterisk in the alpha ‐synuclein immunoblot indicates clusterin bands still present after Clusterin antibody stripping. (d) Clusterin immunoprecipitated from the medium of primary astrocytes treated with alpha ‐synuclein pffs for 16 hr was subjected to immunoblotting using an alpha ‐synuclein antibody. (e) Quantification of clusterin— alpha ‐synuclein pffs interaction has been obtained by normalization of alpha ‐synuclein pffs bound to clusterin for alpha ‐synuclein pffs bound to protein‐G beads. Data are representative of three independent experiments and are expressed as the mean ± SD. Data were analyzed using one‐sample t test; *p = .0493. (f) Z‐stack frames of primary astrocytes treated with alpha ‐synuclein pffs for 16 hr and stained for alpha ‐synuclein (purple), clusterin (green), cadherin (red), and nuclei with DAPI (blue). Scale bar 10 μm. (g) Maximum intensity Z‐projection confocal images of primary astrocytes treated with alpha ‐synuclein pffs for 16 hr and stained for alpha ‐synuclein (purple), clusterin (red), Early Endosome Antigen 1 (EEA1) (green) and nuclei with DAPI (blue). Scale bar 10 μm. Individual points of the graphs represent each single experiment [Color figure can be viewed at wileyonlinelibrary.com] Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33045109), licensed under a CC-BY license. Not internally tested by R&D Systems.")
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