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Manufactured by BioVendor

Clusterin Human NATIVE, Human Plasma

  • Regulatory status:RUO
  • Type:Native protein
  • Source:Plasma
  • Other names:Apolipoprotein J, Apo J
  • Species:Human
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Cat. No. Size Price


RD172034100-S 0.1 mg
PubMed Product Details
Technical Data

Type

Native protein

Description

Native protein purified from human plasma

Source

Plasma

Purity

Purity as determined by densitometric image analysis: >95%

SDS-PAGE Gel

12% SDS-PAGE separation of Human Clusterin
1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa
2. reduced and heated sample, 5μg/lane
3. non-reduced and non-heated sample, 5μg/lane

Endotoxin

< 1.0 EU/ug

Formulation

Filtered (0.4 μm) and lyophilized in 0.5 mg/mL in PBS buffer, pH 7.5

Reconstitution

Add deionized water to prepare a working stock solution of 0.5 mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

Applications

Western blotting, ELISA, Cell culture and/or animal studies

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store the lyophilized protein at –80 °C. Lyophilized protein remains stable until the expiry date when stored at –80 °C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80 °C for long term storage. Reconstituted protein can be stored at 4 °C for a week.

Quality Control Test

BCA to determine quantity of the protein.

SDS PAGE to determine purity of the protein.

LAL to determine quantity of endotoxin.

Note

Material used for protein preparation was tested and found negative for anti-HCV and HIV Ag/Ab. Since no test can absolutely assure the absence of all infectious agents, this product should be handled as a potential biohazard. This product is intended for research use only.

Summary

Research topic

Neural tissue markers, Oncology, Others, Renal disease, Sepsis

Summary

Clusterin is a 75–80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid, but truncated forms targeted to the nucleus have also been identified.

The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the alpha and beta chains. These are assembled anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil alpha-helices and three predicted amphipathic alpha-helices. Clusterin is a heavily N-glycosylated protein.

Across a broad range of species clusterin shows 70% to 80% of sequence homology. It is ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.

It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodelling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.

A detailed mechanism of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced by degraded and misfolded protein precipitates.Clus­terin is up- or downregulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.

Product References (3)

References

  • Novinec M, Lenarčič B, Baici A. Clusterin is a specific stabilizer andliberator of extracellular cathepsin K. FEBS Lett. 2012 Apr 5;586(7):1062-6. doi:10.1016/j.febslet.2012.03.004. Epub 2012 Mar 10. PubMed PMID: 22569264. See more on PubMed
  • Peix L, Evans IC, Pearce DR, Simpson JK, Maher TM, McAnulty RJ. Diversefunctions of clusterin promote and protect against the development of pulmonaryfibrosis. Sci Rep. 2018 Jan 30;8(1):1906. doi: 10.1038/s41598-018-20316-1. PubMedPMID: 29382921; PubMed Central PMCID: PMC5789849. See more on PubMed
  • Prozeller D, Pereira J, Simon J, Mailänder V, Morsbach S, Landfester K.Prevention of Dominant IgG Adsorption on Nanocarriers in IgG-Enriched BloodPlasma by Clusterin Precoating. Adv Sci (Weinh). 2019 Apr 4;6(10):1802199. doi:10.1002/advs.201802199. eCollection 2019 May 17. PubMed PMID: 31131195; PubMedCentral PMCID: PMC6523372. See more on PubMed
Summary References (13)

References to Clusterin

  • Choi-Miura NH, Oda T: Relationship between multifunctional protein Clusterin and Alzheimer disease. Neurobiol. Aging 1996; 17(5): 717–722
  • Newkirk MM, Apostolakos P, Neville C and Fortin PR: Systemic lupus erythematosus, a disease associated with low levels of Clusterin/ApoJ, and anti-inflammatory protein. J. Rheumatol.1999; 3:597–603
  • Morrissey C, Lakins J, Moquin A, Hussain M, Tenniswood M: An antigen capture assay for the measurement of serum Clusterin concentrations. J. Biochen. Biophys. Methods 2001; 48:13–21
  • Trougakos IP, Poulakou M, Stathatos M, Chalikia A, Melidonis A, Gonos ES: Serum levels of the senescence biomarker Clusterin/apolipoprotein J increase significantly in diabetes type II and during development of coronary heart disease or at myocardial infarction. Ex. Gerontology 2002; 37: 1175–1187
  • Jones SE, Jomary C: Molecules in focus Clusterin. The International J. of Bioch. & Cell Biol. 2002; 34:427–431
  • Hidaka S, Kränzlin B, Gretz N, Witzgall R: Urinary Clusterin levels in the rat correlate with the severity of tubular damage and may help to differentiate between glomerular and tubular injuries. Cell Tissue Res. 2002; 310:289–296
  • Chen X, Halberg RB, Ehrhardt WM, Torrealba J and Dove WF: Clusterin as a biomarker in murine and human intestinal neoplasia. PNAS 2003; 100:9530–9535
  • Zhang LY, Ying WT, Mao YS, He HZ, Liu Y, Wang HX, Liu F, Wang K, Zhang DC, Wang Y, Wu M, Qian XH and Zhao XH: Loss of Clusterin both in serum and tissue correlates with the tumorogenesis of esophageal squamous cell carcinoma via proteomics approaches. World J Gastroenterol 2003; 9:650–654
  • Wang L, Erling P, Bengtsson AA, Truedsson L, Sturfelt G, Erlinge D: Transcriptional down-regulation of the platelet ADP receptory P2Y12 and Clusterin in patients with systemic lupus erythematosus. J. of Thromb. And Haemost. 2004; 2:1436–1442
  • Patel NV, Wei M, Wong A, Finch CE, Morgan TE: Progressive changes in regulation of apolipoproteins E and J in glial cultures during postnatal development and aging. Neuroscience Letters 2004; 371:199–204
  • Kim BM, Kim SY, Lee S, Shin YJ, Min BH, Bendayan M, Park IS: Clusterin induces differentiation of pancreatic duct calls into insulin-secreting cells. Diabetologia 2006; 49:311–320
  • Kruger S, Mahnken A, Kausch I, Feller AC: Value of Clusterin immunoreactivity as a predictive factor in muscle-invasive urothelial bladder carcinoma. Urology 2006; 67:105–109
  • Stejskal D, Fiala R: Evaluation of serum and urine Clusterin as a potential tumor marker for urinary bladder cancer. Neoplasma 2006; 53:343–34
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