Recombinant Human Clusterin protein (His tag N-Terminus)

Specifications

Form

Liquid

Additional notes

ab177715 was purified using conventional chromatography techniques.

General info

Function

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).

Sequence similarities

Belongs to the clusterin family.

Post-translational modifications

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).. Polyubiquitinated, leading to proteasomal degradation (PubMed:17451556, PubMed:19137541). Under cellular stress, the intracellular level of cleaved form is reduced due to proteasomal degradation (PubMed:17451556).. Extensively glycosylated with sulfated N-linked carbohydrates (PubMed:17260971, PubMed:2387851). About 30% of the protein mass is comprised of complex N-linked carbohydrate (PubMed:2387851). Endoplasmic reticulum (ER) stress induces changes in glycosylation status and increases level of hypoglycosylated forms (PubMed:22689054). Core carbohydrates are essential for chaperone activity (PubMed:25402950). Non-secreted forms are hypoglycosylated or unglycosylated (PubMed:24073260).

Subcellular localisation

Nucleus