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CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Complement-associated protein SP-40,40, Complement cytolysis inhibitor, NA1/NA2, Apolipoprotein J, Apo-J, Testosterone-repressed prostate message 2, TRPM-2.
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 Rat was constructed as a recombinant protein with N-terminal fusion of T7-Tag (16AA) and C-terminal fusion of His-Tag (9AA). The Clusterin Rat His-Tagged Fusion Protein, produced in E.coli, is 26.5 kDa protein containing 215 amino acid residues of the APO-J Rat and 25 additional amino acid residues – His-Tag, T7-Tag (underlined).
MASMTGGQQM GRDPNSSSPF YFWMNGDRID SLLESDRQQS QVLDAMQDSF TRASGIIDTL FQDRFFTHEPQDIHHFSPMG FPHKRPHLLY PKSRLVRSLM PLSHYGPLSF HNMFQPFFDM IHQAQQAMDV QLHSPALQFPDVDFLKEGED DRTVCKEIRH NSTGCLKMKG QCEKCQEILS VDCSTNNPAQ ANLRQELNDS LQVAERLTQQYNELLHSLQS KMLNTSSLLE QALEHHHHHH
Escherichia Coli.
White lyophilized (freeze-dried) powder.
Lyophilized from 0.5 mg/ml in 0.01M Tris pH 7.2.
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.
Greater than 95% as determined by SDS PAGE.
Elisa, Western blotting
· 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.
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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