ApoJ/Clusterin human

Native Apolipoprotein J (ApoJ), also named Clusterin, is a heavily glycosylated, 75-80 kDa disulfide-linked heterodimeric protein. Despite being cloned since 1989, no genuine function has been attributed to ApoJ so far. The protein has been reportedly implicated in several diverse physiological processes such as sperm maturation, lipid transportation, complement inhibition, tissue remodeling, membrane recycling, cell-cell and cell-substratum interactions, stabilization of stressed proteins in a folding-competent state and promotion or inhibition of apoptosis. ApoJ gene is differentially regulated by cytokines, growth factors and stress-inducing agents. Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.

Lyophilized from 2 mg/mL solution of ApoJ in 25 mM Na2HPO4 and 100 mM NaCl (pH 7.5).

Reconstitute in dH2O to a working concentration of 0.5 mg/mL and let the lyophilized pellet dissolve completely.