Clusterin Human HEK293 Tag free

Cat. No.	Size	Price
RD176034100	0.1 mg

Technical Data

Type

Recombinant protein

Description

Total 427 AA. MW: 50.1 kDa (calculated). NCBI Reference Sequence: P10909 (Asp23-Glu449). Protein identity confirmed by MS.

Amino Acid Sequence

DQTVSDNELQEMSNQGSKYVNKEIQNAVNGVKQIKTLIEKTNEERKTLLSNLEEAKKKKEDALNETRESETKLKELPGVCNETMMALWEECKPCLKQTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLENDRQQTHMLDVMQDHFSRASSIIDELFQDRFFTREPQDTYHYLPFSLPHRRPHFFFPKSRIVRSLMPFSPYEPLNFHAMFQPFLEMIHEAQQAMDIHFHSPAFQHPPTEFIREGDDDRTVCREIRHNSTGCLRMKDQCDKCREILSVDCSTNNPSQAKLRRELDESLQVAERLTRKYNELLKSYQWKMLNTSSLLEQLNEQFNWVSRLANLTQGEDQYYLRVTTVASHTSDSDVPSGVTEVVVKLFDSDPITVTVPVEVSRKNPKFMETVAEKALQEYRKKHREE

Source

HEK293

Purity

˃ 90 % by SDS-PAGE

SDS-PAGE Gel

12 % SDS-PAGE separation of Human Clusterin Human (HEK) tag free:

M.W. marker – 14, 21, 31, 45, 66, 97 kDa
Reduced and boiled sample, 2.5 μg/lane
Non-reduced and non-boiled sample, 2.5 μg/lane

Endotoxin

< 1.0 EU/µg

Formulation

Filtered (0.4 μm) and lyophilized from 0.5 mg/ml solution in phosphate buffered saline, pH 7.5.

Reconstitution

Add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely.

Applications

Western blotting, ELISA

Shipping

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

Storage/Expiration

Store 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. Endotoxin level determination.

Note

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.

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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