|Datasheet||Specific References||Reviews||Related Products||Protocols|
|Recombinant Human Clusterin / Apolipoprotein J / Apo-J / CLU protein (Catalog#11297-H08H)|
|0.2 μm filtered solution in PBS with 5% trehalose|
|This antibody was obtained from a rabbit immunized with purified, recombinant Human Clusterin / Apolipoprotein J / Apo-J / CLU (rh Clusterin / Apolipoprotein J / Apo-J / CLU; Catalog#11297-H08H; NP_001822.2; Met1-Glu501).|
|Human Clusterin / Apolipoprotein J / Apo-J / CLU|
Has cross-reactivity in ELISA with
IHC-P: 1-10 μg/mL
|This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free.|
Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles.
Clusterin, also known as complement-associated protein SP-40, Complement cytolysis inhibitor, Apolipoprotein J, Testosterone-repressed prostate message 2, Aging-associated gene 4 protein, CLU and APOJ, is a secreted protein which belongs to the clusterin family. Clusterin/Apolipoprotein J/Apo-J is an enigmatic glycoprotein with a nearly ubiquitous tissue distribution and an apparent involvement in biological processes ranging from mammary gland involution to neurodegeneration in Alzheimer's disease. Its major form, a heterodimer, is secreted and present in physiological fluids, but truncated forms targeted to the nucleus have also been identified. Clusterin/Apolipoprotein J/Apo-J is a widely distributed glycoprotein with a wide range of biologic properties. A prominent and defining feature of clusterin is its marked induction in such disease states as glomerulonephritis, cystic renal disease, renal tubular injury, neurodegenerative conditions, atherosclerosis, and myocardial infarction. 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.