| Host: |
HEK293 cells |
| Reactivity: |
Mouse |
| Note: |
STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
| Short Description: |
Recombinant-Mouse Clusterin/Apo-J/CLU-C-His protein was developed from hek293 cells and has a target region of C-His. For use in research applications. |
| Formulation: |
Lyophilized 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. |
| Gene Symbol: |
Clu |
| Gene ID: |
12759 |
| Uniprot ID: |
CLUS_MOUSE |
| Immunogen Region: |
Gly21-Glu448 |
| Immunogen: |
Recombinant Mouse Clusterin/Apo-J/CLU Protein is produced by HEK293 cells expression system. The target protein is expressed with sequence (Gly21-Glu448) of mouse Clusterin/Apo-J/CLU (Accession #NP_038520.2) fused with and a 6×His tag at the C-termin |
| 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 | 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. When secreted, 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. Following stress, promotes apoptosis. Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. Following ER stress, suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. When secreted, does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity. When secreted, acts 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. |
| Protein Name | ClusterinApolipoprotein JApo-JClustrinSulfated Glycoprotein 2Sgp-2 Cleaved Into - Clusterin Beta Chain - Clusterin Alpha Chain |
| Database Links | Reactome: R-MMU-114608Reactome: -MMU-166665Reactome: -MMU-6803157Reactome: -MMU-977606 |
| Cellular Localisation | SecretedNucleusCytoplasmMitochondrion MembranePeripheral Membrane ProteinCytoplasmic SideCytosolMicrosomeEndoplasmic ReticulumMitochondrionPerinuclear RegionCytoplasmic VesicleSecretory VesicleChromaffin GranuleCan Retrotranslocate From The Secretory Compartments To The Cytosol Upon Cellular StressDetected In Perinuclear Foci That May Be Aggresomes Containing MisfoldedUbiquitinated ProteinsDetected At The Mitochondrion Membrane Upon Induction Of ApoptosisUnder Er StressA Immaturely Glycosylated Pre-Secreted Form Retrotranslocates From The Endoplasmic Reticulum (Er)-Golgi Network To The Cytoplasm To Localize In The Mitochondria Through Hspa5 InteractionEr Stress Reduces SecretionUnder The StressMinor Amounts Of Non-Secreted Forms Accumulate In Cytoplasm |
| Alternative Protein Names | Clusterin proteinApolipoprotein J proteinApo-J proteinClustrin proteinSulfated Glycoprotein 2 proteinSgp-2 Cleaved Into - Clusterin Beta Chain - Clusterin Alpha Chain proteinClu proteinApoj proteinMsgp-2 protein |
Information sourced from Uniprot.org
12 months for antibodies. 6 months for ELISA Kits. Please see website T&Cs for further guidance
