protein

Recombinant Canine Clusterin, His-tagged

CLU-1318C

Recombinant Canine Clusterin, His-tagged

Creative Biomart

CLU

clusterin

CLU; clusterin; CLI; AAG4; APOJ; CLU1; CLU2; KUB1; SGP2; APO-J; SGP-2; SP-40; TRPM2; TRPM-2; NA1/NA2; apolipoprotein J; ku70-binding protein 1; sulfated glycoprotein 2; aging-associated protein 4; complement lysis inhibitor; complement cytolysis inhibitor; complement-associated protein SP-40,40; testosterone-repressed prostate message 2;

Recombinant Canine Apoliprotein-J produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 433 amino acids and having a molecular mass of 50.6 kDa. The protein is fused to His tag at N-Terminus. The Apoliprotein-J canine is purified by proprietary chromatographic techniques. The amino acids sequence is identical to UniProtKB/Swiss-Prot entry P25473 amino acids 23–445.

Recombinant Canine Apoliprotein-J produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 433 amino acids and having a molecular mass of 50.6 kDa. The protein is fused to His tag at N-Terminus. The Apoliprotein-J canine is purified by proprietary chromatographic techniques. The amino acids sequence is identical to UniProtKB/Swiss-Prot entry P25473 amino acids 23–445.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.

Escherichia Coli

Greater than 95% as determined by SDS PAGE.

P25473