|Application ||WB, IHC-P, IF, E|
|Other Accession||NP_001822, 1191|
|Calculated MW||52495 Da|
|Application Notes||Clusterin antibody can be used for the detection of Clusterin by Western blot at 0.5 - 1 μg/mL. Antibody can also be used for immunohistochemistry starting at 5 μg/mL. For immunofluorescence start at 20 μg/mL.|
|Other Names||Clusterin Antibody: CLI, AAG4, APOJ, CLU1, CLU2, KUB1, SGP2, APO-J, SGP-2, SP-40, TRPM2, TRPM-2, NA1/NA2, CLI, Clusterin, Aging-associated gene 4 protein, Apo-J, clusterin|
|Target/Specificity||Clusterin antibody was raised recombinant human Clusterin isoform 1.|
|Reconstitution & Storage||Clusterin antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.|
|Precautions||Clusterin Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||APOJ, CLI, KUB1|
|Function||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.|
|Cellular Location||Isoform 1: Secreted. Note=Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress|
|Tissue Location||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|
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Provided below are standard protocols that you may find useful for product applications.
Clusterin Antibody: Clusterin, also known as Apolipoprotein J (ApoJ), is a ubiquitous multifunctional glycoprotein that can interact with a broad spectrum of molecules such as complement components, various receptors, and the Alzheimer's b-amyloid peptide. Clusterin expression is increased in Alzheimer's disease brain tissue and clusterin-immunoreactive amyloid plaques are found associated with phospho-tau-positive dystrophic neurites and it has been suggested that clusterin facilitates the conversion of diffuse b-amyloid deposits into amyloid and enhances tau phosphorylation in neurites around these plaques. Other reports show that clusterin expression is decreased in proliferating cells and is upregulated in quiescent and senescent cells, suggesting that it may also play a role in aging and tumorigenesis suppression. Clusterin exists in at least two distinct isoforms.
Calero M, Rostagno A, Frangione B, et al. Clusterin and Alzheimer’s disease. Subcell. Biochem. 2005; 38:273-98.
Martin-Rehrmann MD, Hoe HS, Capuani EM, et al. Association of apolipoprotein J-positive β-amyloid plaques with dystrophic neurites in Alzheimer’s disease brain. Neurotox. Res. 2005; 7:231-42.
Trougakos IP and Gonos ES. Clusterin/Apolipoprotein J in human aging and cancer. Int. J. Biochem. Cell Biol. 2002; 34:1430-48.
Martinon F and Tschopp J. NLRs join TLRs as innate sensors of pathogens. TRENDS Imm. 2005; 26:447-54.
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