Product Details

Purity

>85% (SDS-PAGE)

Target Names

Clu

Uniprot No.

P05371

Alternative Names

CluClusterin; Dimeric acid glycoprotein; DAG; Sulfated glycoprotein 2; SGP-2; Testosterone repressed prostate message 2; TRPM-2) [Cleaved into: Clusterin beta chain; Clusterin alpha chain]

Species

Rattus norvegicus (Rat)

Expression Region

22-447

Target Protein Sequence

EQEFSDNEL QELSTQGSRY VNKEIQNAVQ GVKHIKTLIE KTNAERKSLL NSLEEAKKKK EGALDDTRDS EMKLKAFPEV CNETMMALWE ECKPCLKHTC MKFYARVCRS GSGLVGRQLE EFLNQSSPFY FWMNGDRIDS LLESDRQQSQ VLDAMQDSFT RASGIIDTLF QDRFFTHEPQ DIHHFSPMGF PHKRPHFLYP KSRLVRSLMP LSHYGPLSFH NMFQPFFDMI HQAQQAMDVQ LHSPALQFPD VDFLKEGEDD PTVCKEIRHN STGCLKMKGQ CEKCQEILSV DCSTNNPAQA NLRQELNDSL QVAERLTQQY NELLHSLQSK MLNTSSLLEQ LNDQFTWVSQ LANLTQGDDQ YLRVSTVTTH SSDSEVPSRV TEVVVKLFDS DPITVVLPEE VSKDNPKFMD TVAEKALQEY RRKSRME

Protein Length

Full Length of Mature Protein

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose, pH 8.0

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Target Background

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. 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.

Gene References into Functions

clusterin might be involved in the formation of tubular complexes and parenchymal regeneration during rat pancreatitis PMID: 30111670
Results suggest that an increase in the secretion of clusterin by Sertoli cells protects the testes from heat stress-induced injury. PMID: 25661013
ApoJ serves as a cytoprotective protein in neonatal rat ventricular cells against cytotoxicity of AngII through the PI3K-Akt-ROS and MAPK/ NF-kappaB pathways. PMID: 26391229
rats treated with KD (EXP2) showed a significant down-regulated expression of ZnT-3, MT-3, ApoE, clusterin, and ACAT-1 in hippocampus PMID: 25778834
Following restraint stress, hypothalamic and pituitary clusterin expression levels are augmented. PMID: 24080898
Exendin-4 treatment induces new beta cell clusters via up-regulation of clusterin, which might be effective on beta-cell proliferation and neogenesis. PMID: 23351716
Nulear clusterin plays a pro-apoptotic role in ethanol-induced cell death in the developing brain. PMID: 21762182
Cox-2 induces clusterin in a 15d-PGJ(2)-dependent manner. PMID: 22138303
attenuates renal fibrosis in obstructive nephropathy PMID: 22052058
The results suggested that clusterin may contribute to gastrin's growth-promoting effect on the oxyntic mucosa. PMID: 21995960
bisphenol A upregulated clusterin expression in atrophic prostate epithelial cells and induced lipid peroxidation and DNA fragmentation in spermatozoa. PMID: 21536718
clusterin is an important mediator of neural precursor cell-derived neuronal survival and differentiation PMID: 21212797
The chaperone clusterin mediates systemic clearance of misfolded extracellular proteins PMID: 21505792
The chaperone action of clusterin is independent of ATP PMID: 11123922
The chaperone action of clusterin targets prefibrillar species to inhibit amyloid formation PMID: 17412999
The extracellular chaperone clusterin appears in the cytosol during endoplasmic reticulum stress PMID: 17451556
The chaperone action of clusterin is important in quality control of extracellular protein folding PMID: 19878774
The chaperone clusterin inhibits aggregation and precipitation of major human plasma proteins PMID: 19996109
Clusterin is an extracellular holdase-type chaperone PMID: 10066740
The chaperone action of clusterin is like that of the small heat shock proteins PMID: 10694874
Urinary levels serve as a marker for the severity of tubular damage and may help to differentiate between glomerular and tubular injuries. PMID: 12457227
clusterin production and secretion, particularly by astrocytes, could be neuroprotective-perhaps via its putative actions such as inhibition of complement activation and cytolysis, effects on chemotaxis and apoptosis, and actions as an anti-stress protein PMID: 12782389
clusterin can be involved in neurodegeneration and cell survival PMID: 12799419
Role for TRPM2 in the calcium signaling of activated microglia. PMID: 14512294
After retinal ischemia, some Muller cells die by apoptosis; clusterin produced and released by Muller cells may play an important role in the pathogenesis of ischemic injury in the rat retina. PMID: 15139011
The role of clusterin and its isoforms in SMC behavior is complex and chronologically regulated in response to microenvironmental changes. Proliferative arrest reduces s-CLU; apoptosis increases n-CLU. PMID: 15591223
clusterin protects cardiomyocytes against ischemic cell death via a complement-independent pathway PMID: 15994859
Sclip interacts with clusterin in PC12 cells and the interaction may act as an important modulator during neuronal differentiation. PMID: 16038898
These observations suggest that clusterin induction is NF-kappaB-independent and unrelated to the inflammatory response in N9 microglia. PMID: 16157419
Accumulation of aberrant proteins, caused by the proteasome inhibitor MG132 or the incorporation of the amino acid analogue AZC (L-azetidine-2-carboxylic acid), increased both clusterin protein and mRNA levels in the human glial cell line U-251 MG. PMID: 16336210
results suggest that clusterin can be considered as a potential morphogenic factor that promotes differentiation of pancreatic beta cells PMID: 16411126
Molecular pathological evaluation of clu in a rat model of unilateral ureteral obstruction was made as a possible biomarker of nephrotoxicity. PMID: 17455085
clusterin overexpression is associated with the up-regulation of the phosphorylation of Akt PMID: 18321852
Regulation of clusterin expression in the prostate of aging rats is complex and is neither directly repressed by androgen nor dependent on apoptotic-induced stress PMID: 18942093
Results indicate that secreted clusterin expression in diabetic nephropathy was induced due to renal tissue damage, and the nuclear clusterin expression increase in renal tubuli was related to apoptosis. PMID: 18949565
upregulation of clusterin during vascular injury may be a protective response against, rather than a causative response to, the development of neointimal hyperplasia. PMID: 19696405

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Subcellular Location

Secreted. Nucleus. Cytoplasm. Mitochondrion membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytosol. Microsome. Endoplasmic reticulum. Mitochondrion. Mitochondrion membrane. Cytoplasm, perinuclear region. Cytoplasmic vesicle, secretory vesicle, chromaffin granule.

Protein Families

Clusterin family

Tissue Specificity

Detected in Sertoli cells (at protein level). Detected in cultured Sertoli cells, testis, epididymis, liver and brain.

Database Links

KEGG: rno:24854

STRING: 10116.ENSRNOP00000022095

UniGene: Rn.1780

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Recombinant Rat Clusterin (Clu)

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