Recombinant Mouse Clusterin/ApoJ Protein (His Tag) Purity >95%

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SKU: PKSM041216-50
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Recombinant Mouse Clusterin/ApoJ Protein (His Tag) Purity >95%

 

SKU # PKSM041216
Expression Host HEK293 Cells

 

 

Description

Synonyms ApoJ, Apolipoprotein J, Cli, Clusterin, Clustrin, D14Ucla3, SP-40, Sgp-2, Sgp2, Sugp-2, Sulfated glycoprotein 2
Species Mouse
Expression Host HEK293 Cells
Sequence Glu22-Glu448
Accession Q06890
Calculated Molecular Weight 50.4 kDa
Observed Molecular Weight 28-50&70 kDa
Tag C-His
Bio-activity Not validated for activity
  

 

Properties

Purity > 95 % as determined by reducing SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method.
Storage Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Shipping This product is provided as lyophilized powder which is shipped with ice packs.
Formulation Lyophilized from a 0.2 μm filtered solution of 20mM PB,150mM NaCl,pH7.4.
Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.
Reconstitution Please refer to the printed manual for detailed information.



Background

Clusterin(CLU) is a secreted protein which belongs to the clusterin family. It is also a 75 - 80 kDa disulfide-linked heterodimeric protein associated with the clearance of cellular debris and apoptosis. Clusterin 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. It 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.