rh CLUS / Clusterin is fused with 6 xHis tag at the C terminus, and has a calculated MW of 50.9 kDa (Asp23-Glu449, α chain 24.5 kDa + β chain 27 kDa). The recombinant rh CLUS / Clusterin (Asp23-Glu 449) was cleaved into α chain and β chain, which form a heterodimer linked by disulfide bonds. DTT reduced protein migrates as 39 kDa and 40 kDa bands in SDS-PAGE due to glycosylation, corresponding to the cleaved β chain, and α chain respectively.
CLU
Origine: Rat
Hôte: Escherichia coli (E. coli)
Recombinant
SDS
Restrictions
For Research Use only
Format
Lyophilized
Buffer
PBS, pH 7.4
Conseil sur la manipulation
Please avoid repeated freeze-thaw cycles.
Stock
-20 °C
Stockage commentaire
No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C), After reconstitution under sterile conditions for 3 months (-70 °C).
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 N-glycosylated disulfide-linked 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.