Key features and details
- Sensitivity: 3.399 ng/ml
- Range: 12.5 ng/ml - 800 ng/ml
- Sample type: Plasma, Serum, Urine
- Detection method: Colorimetric
- Assay type: Sandwich (quantitative)
- Reacts with: Rat
Product nameRat Clusterin ELISA Kit (Apolipoprotein J)
See all Apolipoprotein J (Clusterin) kits
Intra-assay Sample n Mean SD CV% Serum < 10% Inter-assay Sample n Mean SD CV% Serum < 10%
Sample typeUrine, Serum, Plasma
Assay typeSandwich (quantitative)
Range12.5 ng/ml - 800 ng/ml
> 85 %
Sample specific recovery Sample type Average % Range Serum > 85 12.5ng/ml - 800ng/ml
Assay durationMultiple steps standard assay
Species reactivityReacts with: Rat
Abcam’s Clusterin (Apolipoprotein J) Rat ELISA Kit is a highly sensitive two-site enzyme linked immunoassay (ELISA) for measuring Clusterin in Rat serum, plasma and urine.
In this assay the Clusterin present in samples reacts with the anti-Clusterin antibodies, which have been adsorbed to the surface of polystyrene microtitre wells. After the removal of unbound proteins by washing, anti-Clusterin antibodies conjugated with horseradish peroxidase (HRP), are added. These enzyme-labeled antibodies form complexes with the previously bound Clusterin. Following another washing step, the enzyme bound to the immunosorbent is assayed by the addition of a chromogenic substrate, 3,3’,5,5’-tetramethylbenzidine (TMB). The quantity of bound enzyme varies directly with the concentration of Clusterin in the sample tested; thus, the absorbance, at 450 nm, is a measure of the concentration of Clusterin in the test sample. The quantity of Clusterin in the test sample can be interpolated from the standard curve constructed from the standards, and corrected for sample dilution.
Components 1 x 96 tests 20X Wash Buffer Concentrate 1 x 50ml 5X Diluent Concentrate 1 x 50ml Chromogen Substrate Solution 1 x 12ml Clusterin (Apolipoprotein J) Rat Antibody coated microwells 1 x 96 tests Clusterin (Apolipoprotein J) Rat Calibrator 1 vial Clusterin (Apolipoprotein J) Rat HRP Conjugate 1 vial Stop Solution 1 x 12ml
RelevanceIsoform 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.
Cellular localizationIsoform 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. 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.
- Aging associated protein 4
- APO J
ab190540 has not yet been referenced specifically in any publications.