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CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.
Clusterin also named Apoliprotein J (APO-J) 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 a and b chains. These are assembled in 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 a-helices and three predicted amphipathic a-helices.
Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly 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 remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
Clusterin is up- or down regulated 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.
The Clusterin Human contains a total 454 amino acids and a calculated molecular mass of 53058Da. The AA sequence (AA 1-427) is identical to Swiss-Prot-P10909 (AA 23-449, secreted Human Clusterin). C-terminal His tag 27AA (bold).
DQTVSDNELQ EMSNQGSKYV NKEIQNAVNG VKQIKTLIEK TNEERKTLLS NLEEAKKKKE DALNETRESE TKLKELPGVC NETMMALWEE CKPCLKQTCM KFYARVCRSGS GLVGRQLEE FLNQSSPFYF WMNGDRIDSL LENDRQQTHM LDVMQDHFSRA SSIIDELFQ DRFFTREPQD TYHYLPFSLP HRRPHFFFPK SRIVRSLMPF SPYEPLNFHA MFQPFLEMIH EAQQAMDIHF HSPAFQHPPT EFIREGDDDR TVCREIRHNS TGCLRMKDQC DKCREILSVD CSTNNPSQAKLRRELDESLQ VAERLTRKYN ELLKSYQWKM LNTSSLLEQL NEQFNWVSRL ANLTQGEDQYYLRVTTVASH TSDSDVPSGV TEVVVKLFDS DPITVTVPVE VSRKNPKFME TVAEKALQEY RKKHREEGSL GSGWSHPQFE KTGHHHHHHH HGGQ
Ni-NTA chromatography.
293 cell line (Human embryonic kidney).
Greater than 95% (SDS PAGE analyzed).
Filtered (0.4 micron) and lyophilized PBS, pH 7.5.
Add 0.2 ml of deionized H2O and let the lyophilized pellet dissolve completely.
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
The lyophilized protein remains stable until the expiry date when stored at -20°C.
· Trougakos IP, Gonos ES. Functional analysis of clusterin/apolipoprotein J in cellular death induced by severe genotoxic stress. Ann N Y Acad Sci. 2004 Jun;1019: 206-10.
· Carver JA, Rekas A, Thorn DC, Wilson MR. Small heat-shock proteins and clusterin: intra- and extracellular molecular chaperones with a common mechanism of action and function? IUBMB Life. 2003 Dec; 55(12): 661-8. Review.
· Min BH, Kim BM, Lee SH, Kang SW, Bendayan M, Park IS. Clusterin expression in the early process of pancreas regeneration in the pancreatectomized rat. J Histochem Cytochem. 2003 Oct; 51(10): 1355-65.
· Park JH, Park JS, Ju SK, Lee KB, Park YK, Kang MH, Na SY, You KH. Clusterin mRNA expression in apoptotic and activated rat thymocytes. Cell Res. 2003 Feb; 13(1): 49-58.
· Jones SE, Jomary C. Clusterin. Int J Biochem Cell Biol. 2002 May; 34(5): 427-31. Review.
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