Rat CLU ELISA Kit | CLU elisa kit
Rat CLU (Clusterin) ELISA Kit
Typical Testing Data/Standard Curve (for reference only)
Principle of the Assay: This ELISA kit uses Sandwich-ELISA as the method. The micro ELISA plate provided in this kit has been pre-coated with an antibody specific to Rat CLU. Standards or samples are added to the appropriate micro ELISA plate wells and bound by the specific antibody. Then a biotinylated detection antibody specific for Rat CLU and Avidin-Horseradish Peroxidase (HRP) conjugate is added to each micro plate well successively and incubated. Free components are washed away. The substrate solution is added to each well. Only those wells that contain Rat CLU, biotinylated detection antibody and Avidin-HRP conjugate will appear blue in color. The enzyme-substrate reaction is terminated by the addition of a sulphuric acid solution and the color turns yellow. The optical density (OD) is measured spectrophotometrically at a wavelength of 450 nm +/- 2 nm. The OD value is proportional to the concentration of Rat CLU. You can calculate the concentration of Rat CLU in the samples by comparing the OD of the samples to the standard curve.
NCBI and Uniprot Product Information
NCBI Description
The protein encoded by this gene is a secreted chaperone that can under some stress conditions also be found in the cell cytosol. It has been suggested to be involved in several basic biological events such as cell death, tumor progression, and neurodegenerative disorders. Alternate splicing results in both coding and non-coding variants.[provided by RefSeq, May 2011]
Uniprot Description
CLU: 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. Belongs to the clusterin family. 5 isoforms of the human protein are produced by alternative splicing.
Protein type: Secreted, signal peptide; Secreted; Mitochondrial; Apoptosis
Chromosomal Location of Human Ortholog: 8p21-p12
Cellular Component: extracellular matrix; Golgi apparatus; extracellular space; mitochondrion; perinuclear region of cytoplasm; endoplasmic reticulum; cytoplasm; mitochondrial membrane; extracellular region; nucleus; cytosol
Molecular Function: protein binding; ubiquitin protein ligase binding; chaperone binding; ATPase activity; misfolded protein binding
Biological Process: platelet activation; release of cytochrome c from mitochondria; response to misfolded protein; positive regulation of nitric oxide biosynthetic process; protein stabilization; positive regulation of apoptosis; response to virus; cell morphogenesis; microglial cell activation; positive regulation of tumor necrosis factor production; activation of NF-kappaB transcription factor; negative regulation of protein homooligomerization; complement activation; platelet degranulation; reverse cholesterol transport; myelin maintenance in the central nervous system; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; protein import; innate immune response; lipid metabolic process; chaperone-mediated protein complex assembly; blood coagulation; complement activation, classical pathway
