Anti-Apolipoprotein J/CLU Antibody Picoband® Fluoro647 Conjugated

Clusterin (apolipoprotein J) is a 75 - 80 kDa disulfide-linked heterodimeric protein associated with the clearance of cellular debris and apoptosis. In humans, clusterin is encoded by the CLU gene. This protein has several synonyms: dimeric acidic glycoprotein (DAG protein), testosterone repressed prostate message-2 (TRPM-2), sulfated glycoprotein-2 (SGP-2) and complement lysis inhibitor (CLI) . Clusterin was mapped to mouse chromosome 14. Clusterin is a ubiquitously expressed molecule thought to influence a variety of processes including cell death. In the brain, it accumulates in dying neurons following seizures and hypoxic-ischemic (H-I) injury. clusterin may be a new therapeutic target to modulate non-caspase-dependent neuronal death following acute brain injury.

Clusterin; Aging-associated gene 4 protein; Apolipoprotein J; Apo-J; Complement cytolysis inhibitor; CLI; Complement-associated protein SP-40,40; Ku70-binding protein 1; NA1/NA2; Testosterone-repressed prostate message 2; TRPM-2; Clusterin beta chain; ApoJalpha; Complement cytolysis inhibitor a chain; Clusterin alpha chain; ApoJbeta; Complement cytolysis inhibitor b chain; CLU; APOJ, CLI, KUB1; AAG4

E. coli-derived human Apolipoprotein J recombinant protein (Position: S228-E449) . Human Apolipoprotein J shares 76.1 % and 75.2 % amino acid (aa) sequence identity with mouse and rat Apolipoprotein J, respectively.

Detected in blood plasma, cerebrospinal fluid, milk, seminal plasma and colon mucosa. Detected in the germinal center of colon lymphoid nodules and in colon parasympathetic ganglia of the Auerbach plexus (at protein level) . Ubiquitous. Detected in brain, testis, ovary, liver and pancreas, and at lower levels in kidney, heart, spleen and lung. .

Cancer, Cardiovascular, Chaperones, Complement, Immunology, Innate Immunity, Lipid Metabolism, Lipids/Lipoproteins, Metabolism, Protein Trafficking, Signal Transduction, Tumor Biomarkers

Isoform 1 functions as extracellular chaperone that prevents aggregation of nonnative proteins. 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. Secreted isoform 1 protects cells against apoptosis and against cytolysis by complement. 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. .

1. Entrez Gene: clusterin. 2. Birkenmeier, E. H., Letts, V. A., Frankel, W. N., Magenheimer, B. S., Calvet, J. P. Sulfated glycoprotein-2 (Sgp-2) maps to mouse chromosome 14. Mammalian Genome 4: 131-132, 1993. 3. Han, B. H., DeMattos, R. B., Dugan, L. L., Kim-Han, J. S., Brendza, R. P., Fryer, J. D., Kierson, M., Cirrito, J., Quick, K., Harmony, J. A. K., Aronow, B. J., Holtzman, D. M. Clusterin contributes to caspase-3-independent brain injury following neonatal hypoxia-ischemia. Nature Med. 7: 338-343, 2001. 4. Jones SE, Jomary C (May 2002) . Clusterin. Int. J. Biochem. Cell Biol. 34 (5) : 427–431.