Clusterin (nuclear form) (human) (rec.) (His)

AdipoGen Life Sciences

Clusterin (nuclear form) (human) (rec.) (His)

10

Research Use Only

1 mg/ml

>90%

Liquid

Clusterin

Clusterin shares homology with the small heat shock protein family of molecular chaperones. The mature secreted form of the protein is a glycosylated, 80-kDa disulfide-linked heterodimer of alpha and beta subunits (produced by internal cleavage). Clusterin is expressed in virtually all tissues and found in all human fluids. It is involved in numerous physiological processes important for carcinogenesis and tumor growth, including apoptotic cell death, cell cycle regulation, DNA repair, cell adhesion, tissue remodeling, lipid transportation, membrane recycling, and immune system regulation. Clusterin also exists as a nuclear protein. The secreted form of Clusterin has extracellular chaperone and anti-apoptotic activities while the nuclear form acts as a proapoptotic factor. - Protein. Human nuclear clusterin (aa 23-449) is fused at the C-terminus to a His-tag. Source: E. coli. Endotoxin content: <1EU/microg purified protein (LAL test; Lonza). Liquid. 0.2microm-filtered solution in 55mM TRIS-Cl, pH 8.2, containing 150mM NaCl. Purity: >90% (SDS-PAGE). Clusterin shares homology with the small heat shock protein family of molecular chaperones. The mature secreted form of the protein is a glycosylated, 80-kDa disulfide-linked heterodimer of alpha and beta subunits (produced by internal cleavage). Clusterin is expressed in virtually all tissues and found in all human fluids. It is involved in numerous physiological processes important for carcinogenesis and tumor growth, including apoptotic cell death, cell cycle regulation, DNA repair, cell adhesion, tissue remodeling, lipid transportation, membrane recycling, and immune system regulation. Clusterin also exists as a nuclear protein. The secreted form of Clusterin has extracellular chaperone and anti-apoptotic activities while the nuclear form acts as a proapoptotic factor.

-20°C,2°C to 8°C

12352202