Human Clusterin / CLUS Protein, His Tag

Proteins and Peptides

貨號 Cat. No.
CLU-H5227
規格 Size
100ug
品牌 Brand
ACROBiosystems
Species
Human
Conjugate
Unconjugated
Expression System
HEK293
Tag
His Tag

Description




Source : 


Human Clusterin, His Tag (CLU-H5227) is expressed from human 293 cells (HEK293). It contains AA Asp 23 - Glu 449 (Accession # NP_001822.3).


 

Molecule : Clusterin


 

Synonyms : CLU,Clusterin,AAG4,APOJ,CLI,KUB1,SGP-2,SP-40,TRPM2


 

Format : Powder


 

Category : Bio-Markers & CD Antigens


 

Accession : NP_001822.3


 

Storage : -20℃


 

Shipping condition : Powder,RT


 

Molecular Weight : 50.9 kDa


 

Characteristics :


This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 50.9 kDa. The protein migrates as 32-40 kDa under reducing (R) condition (SDS-PAGE).


 

Endotoxin Level : Less than 1.0 EU per μg by the LAL method.


 

Buffer : PBS, pH7.4


 

Description :


Clusterin (CLU) is also known as dimeric acidic glycoprotein (DAG protein), testosterone repressed prostate message-2 (TRPM-2), sulfated glycoprotein-2 (SGP-2) and complement lysis inhibitor (CLI), is a secreted multifunctional glycoprotein protein which belongs to the clusterin family. Intracellular cleavages of the precursor of clusterin remove the signal peptide and generate comparably sized α and β chains which are secreted as an 80 kDa N­glycosylated disulfide­linked heterodimer. DAG protein is predominantly expressed in adult testis, ovary, adrenal gland, liver, heart, and brain and in many epithelial tissues during embryonic development. Clusterin involve in several basic biological events such as cell death, tumor progression, and neurodegenerative disorders. Upregulation of clusterin mRNA and protein levels detected in diverse disease states and in in vitro systems have led to suggestions that it functions in membrane lipid recycling, in apoptotic cell death, and as a stress-induced secreted chaperone protein, amongst others.


 

References :


(1) Jones SE., et al., Int. J. Biochem. Cell Biol. 34 (5): 427–431.
(2) Poon S., et al., 2002, J. Biol. Chem. 277:39532-39540.
(3) Leskov K.S., et al., 2003, J. Biol. Chem. 278:11590-11600.
(4) Santilli G., et al., 2003, J. Biol. Chem. 278:38214-38219.
(5) Wong P., et al., 1994, Eur. J. Biochem. 221:917-925.





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