CLU
Origine: Souris
Hôte: Escherichia coli (E. coli)
Recombinant
> 90 %
SDS, WB, Imm, PC
Indications d'application
Optimal working dilution should be determined by the investigator.
Restrictions
For Research Use only
Format
Liquid
Concentration
Lot specific
Buffer
0.2μm-filtered solution in 55 mM TRIS-Cl, pH 8.2, containing 150 mM NaCl.
Stock
4 °C,-20 °C
Stockage commentaire
Short Term Storage: +4°C Long Term Storage: -20°C Working aliquots are stable for up to 3 months when stored at -20°C.
Date de péremption
3 months
Shim, Kang, Jeon, Park, Lee, Lee, Park, Lee, Schedin, Min: "Clusterin induces matrix metalloproteinase-9 expression via ERK1/2 and PI3K/Akt/NF-?B pathways in monocytes/macrophages." dans: Journal of leukocyte biology, Vol. 90, Issue 4, pp. 761-9, (2011) (PubMed).
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.