Text Size:AAA

Clusterin/Apolipoprotein J/Apo-J  Protein, Antibody, ELISA Kit, cDNA Clone

Clusterin/Apolipoprotein J/Apo-J Related Area

Clusterin/Apolipoprotein J/Apo-J Related Pathways

    Clusterin/Apolipoprotein J/Apo-J Related Protein, Antibody, cDNA Gene, and ELISA Kits

    Clusterin/Apolipoprotein J/Apo-J Related Protein, Antibody, cDNA Gene, and ELISA Kits

    Featured Reagent Products

    Clusterin/Apolipoprotein J/Apo-J Summary & Protein Information

    Clusterin/Apolipoprotein J/Apo-J Background

    Subunit structure: Antiparallel disulfide-linked heterodimer of an alpha chain and a beta chain. Self-associates and forms higher oligomers. Interacts with a broad range of misfolded proteins, including APP, APOC2 and LYZ. Slightly acidic pH promotes interaction with misfolded proteins. Forms high-molecular weight oligomers upon interaction with misfolded proteins. Interacts with APOA1, LRP2, CLUAP1 AND PON1. Interacts with the complement complex. Interacts (via alpha chain) with XRCC6. Interacts with SYVN1, COMMD1, BTRC, CUL1 and with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes. Interacts (via alpha chain) with BAX in stressed cells, where BAX undergoes a conformation change leading to association with the mitochondrial membrane. Does not interact with BAX in unstressed cells. Found in a complex with LTF, CLU, EPPIN and SEMG1. {ECO:0000269|PubMed:12047389, ECO:0000269|PubMed:12176985, ECO:0000269|PubMed:12551933, ECO:0000269|PubMed:1491011, ECO:0000269|PubMed:15480429, ECO:0000269|PubMed:1551440, ECO:0000269|PubMed:16113678, ECO:0000269|PubMed:17260971, ECO:0000269|PubMed:17407782, ECO:0000269|PubMed:17412999, ECO:0000269|PubMed:1742316, ECO:0000269|PubMed:17451556, ECO:0000269|PubMed:17567961, ECO:0000269|PubMed:1903064, ECO:0000269|PubMed:19535339, ECO:0000269|PubMed:1974459, ECO:0000269|PubMed:20068069, ECO:0000269|PubMed:2387851, ECO:0000269|PubMed:2780565, ECO:0000269|PubMed:8292612, ECO:0000269|PubMed:8328966}.
    Subcellular location: Isoform 1: Secreted. Note=Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress.; Nucleus. Cytoplasm. Mitochondrion membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytosol. Microsome. Endoplasmic reticulum. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250}. Note=Isoforms lacking the N-terminal signal sequence have been shown to be cytoplasmic and/or nuclear. Secreted isoforms can retrotranslocate from the secretory compartments to the cytosol upon cellular stress. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins. Detected at the mitochondrion membrane upon induction of apoptosis.
    Tissue specificity: 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. {ECO:0000269|PubMed:11123922, ECO:0000269|PubMed:17260971, ECO:0000269|PubMed:17322305, ECO:0000269|PubMed:17412999, ECO:0000269|PubMed:1974459, ECO:0000269|PubMed:2387851, ECO:0000269|PubMed:2780565, ECO:0000269|PubMed:3154963, ECO:0000269|PubMed:8181474, ECO:0000269|PubMed:8292612, ECO:0000269|PubMed:8328966}.
    Induction: Up-regulated in response to enterovirus 71 (EV71) infection (at protein level). Up-regulated by agents that induce apoptosis, both at mRNA and protein level. Isoform 1 is up-regulated by androgen. Isoform 2 is down-regulated by androgen. {ECO:0000269|PubMed:16548883, ECO:0000269|PubMed:17148459, ECO:0000269|PubMed:17689225}.
    Post-translational: Isoform 1 is proteolytically cleaved on its way through the secretory system, probably within the Golgi lumen. {ECO:0000269|PubMed:2387851}.; Polyubiquitinated, leading to proteasomal degradation. {ECO:0000269|PubMed:17451556, ECO:0000269|PubMed:19137541}.; Heavily N-glycosylated. About 30% of the protein mass is comprised of complex N-linked carbohydrate. {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:1551440, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:17260971, ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:2387851, ECO:0000269|PubMed:9336835}.
    Sequence similarity: Belongs to the clusterin family. {ECO:0000305}.
    General information above from UniProt

    Clusterin, also known as complement-associated protein SP-40, Complement cytolysis inhibitor, Apolipoprotein J, Testosterone-repressed prostate message 2, Aging-associated gene 4 protein, CLU and APOJ, is a secreted protein which belongs to the clusterin family. Clusterin/Apolipoprotein J/Apo-J is an enigmatic glycoprotein with a nearly ubiquitous tissue distribution and an apparent involvement in biological processes ranging from mammary gland involution to neurodegeneration in Alzheimer's disease. Its major form, a heterodimer, is secreted and present in physiological fluids, but truncated forms targeted to the nucleus have also been identified. Clusterin/Apolipoprotein J/Apo-J is a widely distributed glycoprotein with a wide range of biologic properties. A prominent and defining feature of clusterin is its marked induction in such disease states as glomerulonephritis, cystic renal disease, renal tubular injury, neurodegenerative conditions, atherosclerosis, and myocardial infarction. Upregulation of clusterin mRNA and protein levels detected in diverse disease states and in in vitro systems have led to suggestions that it functions in membrane lipid recycling, in apoptotic cell death, and as a stress-induced secreted chaperone protein, amongst others.

    Clusterin/Apolipoprotein J/Apo-J Alternative Name

    CLI,AAG4,APOJ,CLU1,CLU2,KUB1,SGP2,APO-J,SGP-2,SP-40,TRPM2,TRPM-2,NA1/NA2, [homo-sapiens]
    AAG4,aging-associated protein 4,APOJ,apo-J,apolipoprotein J,CLI,CLU,Clusterin,complement cytolysis inhibitor,complement lysis inhibitor,KUB1,MGC24903,NA1/NA2,SGP2,SGP-2,SP-40,TRPM2,TRPM-2, [human]
    Apolipoprotein J,AI893575,ApoJ,apo-J,Cli,Clu,Clusterin,clustrin,complement lysis inhibitor,D14Ucla3,Sgp2,Sgp-2,SP-40,Sugp-2,sulfated glycoprotein 2, [mouse]
    Cli,ApoJ,Sgp2,SP-40,Sgp-2,Sugp-2,AI893575,D14Ucla3, [mus-musculus]

    Clusterin/Apolipoprotein J/Apo-J Related Studies

  • Silkensen JR, et al. (1994) The role of clusterin in tissue injury. Biochem Cell Biol. 72(11-12): 483-8.
  • Naik RR, et al. (2002) Biomimetic synthesis and patterning of silver nanoparticles. Nat Mater. 1(3): 169-72.
  • Djeu JY, et al. (2009) Clusterin and chemoresistance. Adv Cancer Res. 105: 77-92.