Recombinant Human Clusterin protein
Recombinant Human Clusterin protein
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Recombinant Human Clusterin protein is a Human Full Length protein, in the 1 to 449 aa range, expressed in HEK 293 cells, with >90%, < 0.1 EU/µg endotoxin level, suitable for SDS-PAGE.
別名を表示する
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
Reactivity data
製品の詳細
Working aliquots are stable for up to 3 months when stored at -20°C.
The secreted form of Apolipoprotein J is a heterodimeric disulfide-linked glycoprotein of 76–80 kDa.
配列情報
出荷温度及び保存条件
出荷温度
短期保存温度
長期保存温度
分注に関する情報
保管に関する情報
補足情報
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
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.
Pathways
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.
製品の性状
製品の状態
Lyophilized
補足情報
ab109150 is 0.2µm filtered
一般的な情報
機能
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).
配列の類似性
Belongs to the clusterin family.
翻訳後修飾
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).
細胞内局在性
Nucleus
ターゲットの情報
Abcam product promise
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