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Description
Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. Intracellular isoforms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity. Nuclear isoforms promote apoptosis. Mitochondrial isoforms suppress BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis. Plays a role in the regulation of cell proliferation. Tissue specificity: Isoform 1: Secreted. Note: Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Mitochondrion membrane, Peripheral membrane protein, Cytoplasmic side. Cytoplasm > cytosol. Microsome. Endoplasmic reticulum. Cytoplasmic vesicle > secretory vesicle > chromaffin granule
Immunogen
A synthetic peptide from aa region 400-448 of mouse Clusterin conjugated to an immunogenic carrier protein was used as the antigen.