Human Clusterin / CLUS Protein, His Tag
Synonym
CLU, Clusterin, AAG4, APOJ, CLI, KUB1, SGP-2, SP-40, TRPM2
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).
Predicted N-terminus: Asp 23
Molecular Characterization
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
Less than 1.0 EU per μg by the LAL method / rFC method.
Purity
>95% as determined by SDS-PAGE.
Formulation
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.
Contact us for customized product form or formulation.
Reconstitution
Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Storage
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
-20°C to -70°C for 12 months in lyophilized state;
-70°C for 3 months under sterile conditions after reconstitution.
Background
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.
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