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Recombinant Mouse CLU, C-6His, Human cells

产品描述

概述

Recombinant Mouse Clusterin is produced by our Mammalian expression system and the target gene encoding Glu22-Glu448 is expressed with a 6His tag at the C-terminus.

使用说明

This material is offered by Novin Biotech for research, laboratory or further evaluation purposes. NOT FOR HUMAN USE.

技术规格

TagC-6His
种属Mouse
表达系统Human cells
Accession#Q06890
SourceHuman Cells
Formulation_DescriptionLyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.4.
StorageLyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.Reconstituted protein solution can be stored at 4-7°C for 2-7 days.Aliquots of reconstituted samples are stable at < -20°C for 3 months.
ReconstitutionDissolve the lyophilized protein in distilled water.
PurityGreater than 85% as determined by reducing SDS-PAGE.
EndotoxinLess than 0.1 ng/μg (1 EU/μg) as determined by LAL test.
BackgroundClusterin(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.
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