Anti-Clusterin Purified Monoclonal Antibody

Clusterin (APO J, SGP-2, TRPM-2, SP-40, pADHC-9, CLJ, T64, GP III, XIP8) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified. It is a conserved secreted glycoprotein expressed by a wide range of tissues and being implicated in many physiological processes, including e.g. lipid transportation, complement inhibition, tissue remodeling, membrane recycling, or clearence of cellular debris. It is nearly ubiqitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen. Clusterin is able to bind and form complexes with numerous partners (immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin etc.) and is expressed in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others. A genuine function of clusterin is still enigmatic.

Complement-associated protein SP-40, Complement cytolysis inhibitor, CLI, CLU, NA1/NA2, Apolipoprotein J, Apo-J, TRPM-2, KBP1, KUB1, CLI, AAG4, APOJ, SGP2

Freshly ejaculated human sperms were washed in PBS and extracted in 3% acetic acid, 10% glycerol, 30 mM benzaminidine. The acid extract was dialyzed against 0.2% acetic acid and subsequently used for immunization. The mouse monoclonal antibody Hs-3 recognizes human clusterin (apolipoprotein J), a conserved secreted glycoprotein.

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.

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.