Recombinant Dog Clusterin (CLU)

Code
MSDS	MSDS Datasheet
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Source
Conjugate
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Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

CLU

Uniprot NO.

P25473

Alternative Names

CLUClusterin; Glycoprotein 80; Gp80) [Cleaved into: Clusterin beta chain; Clusterin alpha chain]

Species

Canis lupus familiaris (Dog) (Canis familiaris)

Source

Yeast

Expression Region

23-445

Target Protein Sequence

DQAVSDTE LQEMSTEGSK YINKEIKNAL KGVKQIKTLI EQTNEERKSL LSNLEEAKKK KEDALNDTKD SETKLKASQG VCNDTMMALW EECKPCLKQT CMKFYARVCR SGSGLVGHQL EEFLNQSSPF YFWMNGDRID SLLENDRQQT HALDVMQDSF NRASSIMDEL FQDRFFTREP QDTYHYSPFS LFQRRPFFNP KFRIARNIIP FPRFQPLNFH DMFQPFFDMI HQAQQAMDVN LHRIPYHFPI EFPEEDNRTV CKEIRHNSTG CLKMKDQCEK CQEILSVDCS SNNPAQVQLR QELSNSLQIA EKFTKLYDEL LQSYQEKMFN TSSLLKQLNE QFSWVSQLAN LTQSEDPFYL QVTTVGSQTS DSNVPVGFTK VVVKLFDSDP ITVMIPEAVS RNNPKFMETV AEKALQEYRQ KHREE
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

Full Length of Mature Protein

Tag Info

N-terminal His-tagged/Tag-Free
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.

Storage Condition

Store at -20°C, for extended storage, conserve at -20°C or -80°C.

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.

Notes

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

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Target Background

Function(From Uniprot)

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

Real time RT-PCR and western blotting analysis indicated there was a greater abundance of clusterin in cryptorchid dog testes. Furthermore, clusterin was detected in extracellular regions of cryptorchid dog testes. PMID:29678567
Clusterin may potentially serve as a marker for chronic spinal cord disease in the dog. PMID:23990410
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 mediates systemic clearance of extracellular misfolded proteins PMID:21505792
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
The chaperone action of clusterin is independent of ATP PMID:11123922
Clusterin expression may increase cardiac progenitor cell migration via increasing CXCR4 expression and SDF-1/chemokine receptor signaling in a PI3/Akt-dependent manner. PMID:20813109

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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

Database Links

UNIGENE: Cfa.1254

KEGG: cfa:442971

STRING: 9615.ENSCAFP00000012350

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