| Host: | HEK293 cells |
| Note: | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
| Formulation: | Lyophilised from a 0.22 Mu m filtered solution of PBS, pH 7.4. |
| Storage Instruction: | Store at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles. |
| Determination Method: | < 0.1 EU/Mu g of the protein by LAL method. |
| Gene Symbol: | CLU |
| Gene ID: | 1191 |
| Uniprot ID: | CLUS_HUMAN |
| Immunogen: | Recombinant Human Clusterin/Apo-J/CLU Protein is produced by HEK293 expression system. The target protein is expressed with sequence (Asp23-Arg227 ( Beta chain) &Ser228-Glu449 ( Alpha chain) ) of human Clusterin/Apolipo J/Apo-J/CLU (Accession #NP_001 |
| Immunogen Sequence: | DQTVSDNELQEMSNQGSKYV NKEIQNAVNGVKQIKTLIEK TNEERKTLLSNLEEAKKKKE DALNETRESETKLKELPGVC NETMMALWEECKPCLKQTCM KFYARVCRSGSGLVGRQLEE FLNQSSPFYFWMNGDRIDSL LENDRQQTHMLDVMQDHFSR ASSIIDELFQDRFFTREPQD TYHYLPFSLPHRRPHFFFPK SRIVRSLMPFSPYEPLNFHA MFQPFLEMIHEAQQAMDIH |
| Tissue Specificity | 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. |
| Post Translational Modifications | Proteolytically cleaved on its way through the secretory system, probably within the Golgi lumen. Proteolytic cleavage is not necessary for its chaperone activity. All non-secreted forms are not proteolytically cleaved. Chaperone activity of uncleaved forms is dependent on a non-reducing environment. Polyubiquitinated, leading to proteasomal degradation. Under cellular stress, the intracellular level of cleaved form is reduced due to proteasomal degradation. Extensively glycosylated with sulfated N-linked carbohydrates. About 30% of the protein mass is comprised of complex N-linked carbohydrate. Endoplasmic reticulum (ER) stress induces changes in glycosylation status and increases level of hypoglycosylated forms. Core carbohydrates are essential for chaperone activity. Non-secreted forms are hypoglycosylated or unglycosylated. |
| Function | Isoform 1: Functions as extracellular chaperone that prevents aggregation of non native 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. Protects cells against apoptosis and against cytolysis by complement. 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. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity. A mitochondrial form suppresses BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity. Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3. Plays a role in the clearance of immune complexes that arise during cell injury. 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. Promotes cell death through interaction with BCL2L1 that releases and activates BAX. |
| Protein Name | Clusterin Aging-Associated Gene 4 Protein Apolipoprotein J Apo-J Complement Cytolysis Inhibitor Cli Complement-Associated Protein Sp-40 -40 Ku70-Binding Protein 1 Na1/Na2 Sulfated Glycoprotein 2 Sgp-2 Testosterone-Repressed Prostate Message 2 Trpm-2 Cleaved Into - Clusterin Beta Chain Apojalpha Complement Cytolysis Inhibitor A Chain Sp-40 -40 Beta-Chain - Clusterin Alpha Chain Apojbeta Complement Cytolysis Inhibitor B Chain Sp-40 -40 Alpha-Chain |
| Database Links | Reactome: R-HSA-114608 Reactome: R-HSA-166665 Reactome: R-HSA-6803157 Reactome: R-HSA-977606 |
| Cellular Localisation | Isoform 1: Secreted Can Retrotranslocate From The Secretory Compartments To The Cytosol Upon Cellular Stress Isoform 4: Cytoplasm Keeps Cytoplasmic Localization In Stressed And Unstressed Cell Isoform 6: Cytoplasm Nucleus Cytoplasm Mitochondrion Membrane Peripheral Membrane Protein Cytoplasmic Side Cytosol Microsome Endoplasmic Reticulum Mitochondrion Perinuclear Region Cytoplasmic Vesicle Secretory Vesicle Chromaffin Granule Secreted Isoforms Can Retrotranslocate From The Secretory Compartments To The Cytosol Upon Cellular Stress Detected In Perinuclear Foci That May Be Aggresomes Containing Misfolded Ubiquitinated Proteins Detected At The Mitochondrion Membrane Upon Induction Of Apoptosis Under Er Stress A Immaturely Glycosylated Pre-Secreted Form Retrotranslocates From The Endoplasmic Reticulum (Er)-Golgi Network To The Cytoplasm To Localize In The Mitochondria Through Hspa5 Interaction Er Stress Reduces Secretion Under The Stress Minor Amounts Of Non-Secreted Forms Accumulate In Cytoplasm Non-Secreted Forms Emerge Mainly From Failed Translocation Alternative Splicing Or Non-Canonical Initiation Start Codon |
| Alternative Protein Names | Clusterin protein Aging-Associated Gene 4 Protein protein Apolipoprotein J protein Apo-J protein Complement Cytolysis Inhibitor protein Cli protein Complement-Associated Protein Sp-40 -40 protein Ku70-Binding Protein 1 protein Na1/Na2 protein Sulfated Glycoprotein 2 protein Sgp-2 protein Testosterone-Repressed Prostate Message 2 protein Trpm-2 Cleaved Into - Clusterin Beta Chain protein Apojalpha protein Complement Cytolysis Inhibitor A Chain protein Sp-40 -40 Beta-Chain - Clusterin Alpha Chain protein Apojbeta protein Complement Cytolysis Inhibitor B Chain protein Sp-40 -40 Alpha-Chain protein CLU protein APOJ protein CLI protein KUB1 protein AAG4 protein |
Information sourced from Uniprot.org