Recombinant Human Clusterin protein is a Human Full Length protein, in the 23 to 449 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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Isoform 1. Functions as extracellular chaperone that prevents aggregation of non native proteins (PubMed:11123922, PubMed:19535339). Prevents stress-induced aggregation of blood plasma proteins (PubMed:11123922, PubMed:12176985, PubMed:17260971, PubMed:19996109). Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro) (PubMed:12047389, PubMed:17407782, PubMed:17412999). Does not require ATP (PubMed:11123922). Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70 (PubMed:11123922). Does not refold proteins by itself (PubMed:11123922). Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation (PubMed:21505792). Protects cells against apoptosis and against cytolysis by complement (PubMed:2780565). Intracellular forms 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 (PubMed:20068069). Promotes proteasomal degradation of COMMD1 and IKBKB (PubMed:20068069). Modulates NF-kappa-B transcriptional activity (PubMed:12882985). A mitochondrial form suppresses BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis (PubMed:16113678, PubMed:17689225). Plays a role in the regulation of cell proliferation (PubMed:19137541). An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5 (PubMed:22689054). Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (PubMed:24073260). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity). Isoform 6. Does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity. Isoform 4. Does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (PubMed:24073260). Promotes cell death through interaction with BCL2L1 that releases and activates BAX (PubMed:21567405).
APOJ, CLI, KUB1, AAG4, CLU, Clusterin, Aging-associated gene 4 protein, Apolipoprotein J, Complement cytolysis inhibitor, Ku70-binding protein 1, NA1/NA2, Sulfated glycoprotein 2, Testosterone-repressed prostate message 2, Apo-J, SGP-2, TRPM-2
Recombinant Human Clusterin protein is a Human Full Length protein, in the 23 to 449 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.3152% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab177715 was purified using conventional chromatography techniques.
Isoform 1
Belongs to the clusterin family.
Proteolytically cleaved on its way through the secretory system, probably within the Golgi lumen (PubMed:2387851). Proteolytic cleavage is not necessary for its chaperone activity (PubMed:25402950). All non-secreted forms are not proteolytically cleaved (PubMed:24073260). Chaperone activity of uncleaved forms is dependent on a non-reducing environment (PubMed:25402950).
Clusterin also known as Apolipoprotein J (ApoJ) is a glycoprotein with a mass of approximately 75-80 kDa. Scientists find clusterin expressed widely in the human body including the brain kidney and reproductive organs. This protein exists in two isoforms a secreted form and a nuclear form each with different locations and functions within the cells.
Clusterin plays multiple roles particularly in lipid transport apoptosis and cell-cell interactions. It does not form part of a larger protein complex but it acts as a molecular chaperone that helps in folding and clearance of damaged proteins. This capability allows clusterin to protect cells against stress conditions such as oxidative stress by preventing abnormal protein aggregation.
Clusterin is involved in pathways related to cell survival and lipid metabolism. It plays a role in the insulin signaling pathway and interacts with proteins like Heat Shock Protein 70 (HSP70) to assist in protein folding and in the activation of apoptotic pathways when needed. Clusterin's function in these processes helps in maintaining cellular homeostasis.
Scientists associate clusterin with Alzheimer’s disease and cancer progression. Elevated levels of clusterin have been observed in Alzheimer's patients suggesting a role in amyloid-beta plaque formation. In cancer clusterin expression influences tumor progression and resistance to therapies. Its interaction with other proteins such as Bax modulates the apoptotic pathways impacting cancer cell survival and chemotherapy resistance.
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15% SDS-PAGE analysis of ab177715 (3μg).
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