Rat Clusterin ELISA

DescriptionBA2011 Format96 wells Measuring range128 - 2 ng/ml Price485 € Certificate of origin Application notes Product Data Sheetdownload .pdf Safety Data Sheetdownload .pdf

Clusterin (Apolippoprotein J; SP-40,40; TRPM-2; SGP-2; pADHC-9; CLJ; T64; GP III; XIP8) is a highly conserved disulfide-linked secreted heterodimeric glycoprotein of 75-80 kDa but truncated forms targeted to nucleus have also been identified.

Clusterin is highly conserved across species, showing 70-80% identity at the amino acid level amongst mammals, and numerous variants and isoforms have been described. The protein is constitutively secreted by a number of cell types including epithelial and neuronal cells and is a major protein in physiological fluids including plasma, milk, urine, cerebrospinal fluid and semen. Due to its wide tissue distribution many diverse physiological functions have been attributed to clusterin including sperm maturation, membrane recycling, lipid transportation, tissue remodelling, complement inhibition and cell-cell or cell-substratum interactions. Moreover, it was proposed, that clusterin functions is as an extra cellular chaperon that stabilizes stressed proteins in a folding-competent state and protein has also been implicated in programmed cell death. Another defining prominent of clusterin is its induction in many severe physiological disturbances states including kidney degenerative diseases, prostate and vesicle carcinogenesis, ovarian cancer and several neurodegenerative conditions.

Interesting study determine that urinary clusterin levels in the rat correlate with severity of tubular damage and may help to differentiate between glomerular and tubular injuries.

Clusterin (Apolippoprotein J; SP-40,40; TRPM-2; SGP-2; pADHC-9; CLJ; T64; GP III; XIP8) is a highly conserved disulfide-linked secreted heterodimeric glycoprotein of 75-80 kDa but truncated forms targeted to nucleus have also been identified.

Clusterin is highly conserved across species, showing 70-80% identity at the amino acid level amongst mammals, and numerous variants and isoforms have been described. The protein is constitutively secreted by a number of cell types including epithelial and neuronal cells and is a major protein in physiological fluids including plasma, milk, urine, cerebrospinal fluid and semen. Due to its wide tissue distribution many diverse physiological functions have been attributed to clusterin including sperm maturation, membrane recycling, lipid transportation, tissue remodelling, complement inhibition and cell-cell or cell-substratum interactions. Moreover, it was proposed, that clusterin functions is as an extra cellular chaperon that stabilizes stressed proteins in a folding-competent state and protein has also been implicated in programmed cell death. Another defining prominent of clusterin is its induction in many severe physiological disturbances states including kidney degenerative diseases, prostate and vesicle carcinogenesis, ovarian cancer and several neurodegenerative conditions.

Interesting study determine that urinary clusterin levels in the rat correlate with severity of tubular damage and may help to differentiate between glomerular and tubular injuries.

Enzyme Immunoassay for the quantitative determination Clusterin in rat serum and urine.

RESOURCES

  1. Hidaka S, Kränzlin B, Gretz N, Witzgall R: Urinary clusterin levels in the rat correlate with the severity of tubular damage and may help to differentiate between glomerular and tubular injuries. Cell Tissue Res, 2002 Oct, 310:289-296
  2. Jones SE, Jomary C: Molecules in focus Clusterin. The International J of Bioch  Cell Biol, 2002 May, 34: 427-431
  3. DeMattos RB, O´dell MA, Parsadanian M, Taylor JW, Harmony JAK, Bales KR, Paul SM, Aronow BJ and Holtzman DM: Clusterin promotes amyloid plaque formation and is critical for neurotic toxicity in a mouse model of Alzheimer´s disease. Proc Natl Acad Sci, 2002 Aug, 99: 10843-10848
  4. Chen X, Halberg RB, Ehrhardt WM, Torrealba J and Dove WF: Clusterin as a biomarker in murine and human intestinal neoplasia. Proc Natl Acad Sci, 2003 Aug, 100: 9530-9535
  5. Min BH, Kim BM, Lee SH, Kang SW, Bendayan M. and Park IS: Clusterin expression in the early process of pancreas regeneration in the pancreatectomized Rat. The J of Histochem  Cytochem, 2003, 51(10): 1355-1365
  6. Trougokos IP, Gonos ES: Functional analysis of clusterin/apolipoprotein J in cellular death induced by severe genotoxic stress. Ann NZ Acad Sci, 2004 Jun, 19:206-210
  7. Krijnen PAJ, Cillessen SAGM, Manoe R, Muller A, Visser CA, Meijer CJLM, Musters RJP, Hack CE, Aarden LA, and Niessen HWM: Clusterin: a protective mediator for ischemic cardiomyocytes? Am J Physiol Heart Circ Physiol 2005; 289:H2193-H2202
  8. Kim BM, Kim SY, Lee S, Shin YJ, Min BH, Bendayan M, Park IS: Clusterin induces differentiation of pancreatic duct calls into insulin-secreting cells. Diabetologia 2006; 49:311-320
  9. Kruger S, Mahnken A, Kausch I, Feller AC: Value of Clusterin immunoreactivity as a predictive factor in muscle-invasive urothelial bladder carcinoma. Urology 2006; 67:105-109
  10. Rodriguez-Pineiro AM, De la Cadena MP, Lopez-Saco A, and Rodriguez-Berrocal FJ: Differential Expression of serum clusterin isoforms in colorectal cancer. Mol. And Cel. Proteomics 2006; 5:1647-1657
  11. Strochi P, Smith MA, Perry G, Tamagno E, Danni O, Pession A, Gaiba A, Dozza B: Clusterin up-regulation following sub-lethal oxidative stress and lipid peroxidation in human neuroblastoma cells. Neurobiol. of Aging 2006; 27:1588-1594
  12. Ishii A, Sakai Y, and Nakamura A: Molecular pathological evaluation of clusterin in a rat model of unilateral ureteral obstruction as a possible biomarker of nephrotoxicity. Toxicologic Pathology 2007; 35:376-382
  13. Stoop MP, Dekker LJ, Titulaer MK, Burgers PC, Sillevis Smitt PAE, Luider TM, and Hintzen RQ: Multiple sclerosis-related identified in cerebrospinal fluid by advanced mass spectrometry. Proteomics 2008; 8:0000-0000

 

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