Anti-Clusterin / Apolipoprotein J / APO-J, clone CLU/4731

1 mg/ml in 1X PBS, BSA free, sodium azide free. Clusterin, also designated complement lysis inhibitor (CLI), apolipoprotein J (APOJ), sulfated glycoprotein 2 (SGP2), SP40 and testosterone-repressed prostate message 2 (TRPM2), is a secretory, heterodimeric glycoprotein that influences immune regulation, cell adhesion, transformation, lipid transportation, tissue remodeling, membrane recycling and cell-cell interactions. Clusterin is synthesized as a 449 amino acid polypeptide that is post-translationally cleaved at an internal bond between Arg 227 and Ser 228. The beta subunit corresponds to residues 23-227. The alpha subunit corresponds to residues 228-449. Overexpression of Clusterin appears to be more common in late stages of mammary tumor progression. Clusterin markedly influences Amyloid structure and neuritic toxicity in vivo and may influence Alzheimer s pathogenesis. Protein function: [Isoform 1]: Functions as extracellular chaperone that prevents aggregation of non native proteins (PubMed:11123922, PubMed:19535339). Prevents stress-induced aggregation of blood plasma proteins (PubMed:11123922, PubMed:12176985, PubMed:17260971, PubMed:19996109). Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro) (PubMed:12047389, PubMed:17407782, PubMed:17412999). Does not require ATP (PubMed:11123922). Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70 (PubMed:11123922). Does not refold proteins by itself (PubMed:11123922). Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation (PubMed:21505792). Protects cells against apoptosis and against cytolysis by complement (PubMed:2780565). Intracellular forms 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 (PubMed:20068069). Promotes proteasomal degradation of COMMD1 and IKBKB (PubMed:20068069). Modulates NF-kappa-B transcriptional activity (PubMed:12882985). A mitochondrial form suppresses BAX- dependent release of cytochrome c into the cytoplasm and inhibit apoptosis (PubMed:16113678, PubMed:17689225). Plays a role in the regulation of cell proliferation (PubMed:19137541). An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5 (PubMed:22689054). Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (PubMed:24073260). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3. Plays a role in the clearance of immune complexes that arise during cell injury. [The UniProt Consortium]