- Regulatory Status
- Other Names
- Complement Lysis Inhibitor (CLI), Apolipoprotein J (APOJ) , Complement associated protein SP-40, 40 (SP-40), Testosterone-repressed prostate message 2 (TRPM2), Sulfated glycoprotein 2 (SGP-2), AAG4, CLU1, CLU2, KUB1
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- Product Citations
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Clusterin, also known as Apolipoprotein J, is a heterodimeric glycoprotein that exhibits a wide array of biological functions including lipid transportation, cell death, cell clustering, complement inhibition, tissue remodeling, reproduction, and cancer progresion. Structurally, alpha (Ser228-Glu449) and beta chain (Asp23-Arg227) of mature clusterin are assembled in an anti-parallel fashion, in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two coiled-coil alpha-helices and three amphipathic alpha-helices. The two chains are coded in a single open reading frame. In blood, circulating clusterin is predominantly associated with HDL. Approximately 22% of clusterin is present in HDL, while only about 9% is present in LDL/VLDL. Insulin resistance, obesity, and dyslipidemia are characteristics of the metabolic syndrome and type 2 diabetes. It has been shown that there is a strong negative correlation between the concentration of clusterin in HDL and both insulin sensitivity and body max index. Thus, clusterin depletion may contribute to the loss of HDL's cardioprotective properties. In fact, clusterin levels in HDL3 increase when patients with cardiovascular diseases are treated with statin and niacin therapy. Importanly, it was shown that people who already have Alzheimer's disease have more clusterin in their blood, and that their clusterin levels correlate with faster cognitive decline in patients sufferring from Alzheimer's disease. These clinical findings suggest that Clusterin may play a role in protein folding. Mature human clusterin shares a 77% amino acid sequence homology with its mouse counterpart.Product Details
- Human Clusterin, amino acids (Asp23-Arg227-beta chain & Ser228-Glu449-alpha chain) (Accession# NP_001822), was expressed with a C-terminal His tag in 293E cells.
- Molecular Mass
- The 433 amino acid recombinant protein has a predicted molecular mass of approximately 50.8 kD. The protein migrates approximately at 40 kD in DTT-reducing conditions and at 70 kD in non-reducing conditions by SDS-PAGE. The predicted N-terminal amino acid is Asp.
- >95%, as determined by Coomassie stained SDS-PAGE.
- 0.22 µm filtered protein solution is in PBS, pH 7.2.
- Endotoxin Level
- Less than 0.1 EU per µg of protein as determined by the LAL method.
- 10 and 25 µg sizes are bottled at 200 µg/mL. 100 µg size and larger sizes are lot-specific and bottled at the concentration indicated on the vial. To obtain lot-specific concentration and expiration, please enter the lot number in our Certificate of Analysis online tool.
- Storage & Handling
- Unopened vial can be stored between 2°C and 8°C for up to 2 weeks, at -20°C for up to six months, or at -70°C or colder until the expiration date. For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored at -20°C or colder. Stock solutions can also be prepared at 50 - 100 µg/mL in appropriate sterile buffer, carrier protein such as 0.2 - 1% BSA or HSA can be added when preparing the stock solution. Aliquots can be stored between 2°C and 8°C for up to one week and stored at -20°C or colder for up to 3 months. Avoid repeated freeze/thaw cycles.
- Human Clusterin is able to bind HDL in a dose dependent manner with an ED50 of 0.5 - 4.0 µg/ml. In addition, hClusterin can block the hEGF (20 ng/ml) induced LnCap cell proliferation in a dose depedent manner with an ED50 of 0.1 - 0.6 ng/ml.
- Application Notes
BioLegend carrier-free recombinant proteins provided in liquid format are shipped on blue-ice. Our comparison testing data indicates that when handled and stored as recommended, the liquid format has equal or better stability and shelf-life compared to commercially available lyophilized proteins after reconstitution. Our liquid proteins are verified in-house to maintain activity after shipping on blue ice and are backed by our 100% satisfaction guarantee. If you have any concerns, contact us at firstname.lastname@example.org.
- Application References
- Zhou W, et al. 2002. Life Sciences 72:11.
- Jenne DE, et al. 1991. J. Biol. Chem. 266:11030.
Ovary, testis, adrenal gland, heart, liver, brain, epithelial tissue, and Sertoli cells.
- Clusterin exhibits functions of lipid transportation, apoptosis, complement inhibition, and tissue remodeling.
- Clusterin is able to bind HDL and inhibit the hEGF induced LnCap cell proliferation in a dose dependent manner.
- Biology Area
- Antigen References
1. de Silva H.V., et al. 1990. J. Biol. Chem. 265:14292.
2. Jenne DE, et al. 1991. J. Biol. Chem. 266:11030.
3. Shannan B, et al. 2006. Cell Death Differ. 13:12.
4. Green PS, et al. 2008. Circulation 118:1259.
5. Falgarone G and Chiocchia G. 2009. Adv. Cancer Res. 104:139.
6. Klock G, et al. 2009. Adv. Cancer Res. 104:115.
7. Hoofnagle AN, et al. 2010. Arterioscler Thromb. Vasc. Biol. 30:2528.
8. Schrijvers EM, et al. 2011. JAMA 305:1322.
- Gene ID
- 1191 View all products for this Gene ID
- View information about Clusterin on UniProt.org
- Why choose BioLegend recombinant proteins?
• Each lot of product is quality-tested for bioactivity as indicated on the data sheet.
• Greater than 95% Purity or higher, tested on every lot of product.
• 100% Satisfaction Guarantee for quality performance, stability, and consistency.
• Ready-to-use liquid format saves time and reduces challenges associated with reconstitution.
• Bulk and customization available. Contact us.
• Learn more about our Recombinant Proteins.
- How does the activity of your recombinant proteins compare to competitors?
We quality control each and every lot of recombinant protein. Not only do we check its bioactivity, but we also compare it against other commercially available recombinant proteins. We make sure each recombinant protein’s activity is at least as good as or better than the competition’s. In order to provide you with the best possible product, we ensure that our testing process is rigorous and thorough. If you’re curious and eager to make the switch to BioLegend recombinants, contact your sales representative today!
- What is the specific activity or ED50 of my recombinant protein?
The specific activity range of the protein is indicated on the product datasheets. Because the exact activity values on a per unit basis can largely fluctuate depending on a number of factors, including the nature of the assay, cell density, age of cells/passage number, culture media used, and end user technique, the specific activity is best defined as a range and we guarantee the specific activity of all our lots will be within the range indicated on the datasheet. Please note this only applies to recombinants labeled for use in bioassays. ELISA standard recombinant proteins are not recommended for bioassay usage as they are not tested for these applications.
- Have your recombinants been tested for stability?
Our testing shows that the recombinant proteins are able to withstand room temperature for a week without losing activity. In addition the recombinant proteins were also found to withstand four cycles of freeze and thaw without losing activity.
- Does specific activity of a recombinant protein vary between lots?
Specific activity will vary for each lot and for the type of experiment that is done to validate it, but all passed lots will have activity within the established ED50 range for the product and we guarantee that our products will have lot-to-lot consistency. Please conduct an experiment-specific validation to find the optimal ED50 for your system.
- How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?
Use formula Specific activity (Units/mg) = 10^6/ ED50 (ng/mL)