Human Clusterin, His Tag is fused with 6 ×His tag at the C terminus, and has a calculated MW of 50.9 kDa (Asp 23 - Glu 449, α chain 24.5 kDa + β chain 27 kDa). The Human Clusterin, His Tag (Asp 23 - 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.
Less than 1.0 EU per μg by the LAL method.
>90% as determined by SDS-PAGE.
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally trehalose is added as protectant before lyophilization.
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Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
No activity loss was observed after storage at:
-20°C to -70°C for 12 months in lyophilized state;
-70°C for 3 months under sterile conditions after reconstitution.
Human Clusterin, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 90%.
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.