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Recombinant Coturnix coturnix japonica Clusterin (CLU)

Recombinant Coturnix coturnix japonica Clusterin (CLU)

Code
MSDS	MSDS Datasheet
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Source
Conjugate
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Product Details
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Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

CLU

Uniprot NO.

P14018

Alternative Names

CLU; T64Clusterin; 51.5 kDa protein) [Cleaved into: Clusterin beta chain; Clusterin alpha chain]

Species

Coturnix japonica (Japanese quail) (Coturnix coturnix japonica)

Source

Yeast

Expression Region

19-451

Target Protein Sequence

QG LVPPNELKQL SAAGSKYIDA EVENAINGVK QMKTLMDKTS KEHQAMLHTL EETKKKKEEA VKLALEKEKQ LAEKQEVCNE TMLSLWEECK PCLKHTCMRV YSKMCHSGSG LVGRQLEEFL NRSSPFSIWV NGERIDDLLD REQRQERRFE DLEERFGLME DGVEDIFQDS TQLYGPAFPF FRTPPFGGFR EAFVPPVQRV HLVPRRRLSR ELHPFFQHPM HGFHRLFQPL FEMTQHMLDG GHGAWEHPLG GFATESRNFS TDRMVCREIR RNSAGCLRMR DECEKCREIL AVDCSQTDPV QSQLREQFED ALRLAERFTR RYDDLLSAFQ AEMLNTSSLL DQLNRQFGWV SRLGNLTQGN DGFLQVTTVF SKTPNLEDPS APADTQVTVQ LFDSEPLSLT VPGDISWDDP RFMEIVAEQA LQHYKQNNTI E
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.

Customer Reviews and Q&A

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Target Background

Function(From Uniprot)

Functions as extracellular chaperone that prevents aggregation of nonnative proteins. Prevents stress-induced aggregation of blood plasma proteins. 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. Modulates NF-kappa-B transcriptional activity. Promotes apoptosis when in the nucleus. 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.

Subcellular Location

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

Protein Families

Clusterin family

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