Clusterin Canine

Clusterin, also known as Apolipoprotein J (APO-J), is a protein with a molecular weight of 75-80 kDa. It exists as a disulfide-linked heterodimer and is heavily glycosylated, containing approximately 30% N-linked carbohydrates rich in sialic acid. However, truncated forms of Clusterin that are targeted to the nucleus have also been identified. The precursor polypeptide chain undergoes proteolytic cleavage, removing the 22-amino acid secretory signal peptide and subsequently separating the a and b chains between residues 227 and 228. These chains assemble in an anti-parallel orientation, forming a heterodimeric molecule. Within the molecule, five disulfide bridges connect cysteine-rich centers, which are flanked by two predicted coiled-coil alpha-helices and three predicted amphipathic alpha-helices. Clusterin exhibits a high degree of sequence homology across a wide range of species, with similarities ranging from 70% to 80%. Its expression is nearly ubiquitous in most mammalian tissues, and it can be found in various bodily fluids, including plasma, milk, urine, cerebrospinal fluid, and semen. Clusterin possesses the ability to bind to and form complexes with numerous molecules, including immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta-amyloid, leptin, and others. Numerous functions have been attributed to Clusterin, such as phagocyte recruitment, aggregation induction, prevention of complement attack, inhibition of apoptosis, membrane remodeling, lipid transport, hormone transport and/or scavenging, and matrix metalloproteinase inhibition. Despite extensive research, a definitive function of Clusterin remains elusive. One compelling hypothesis proposes that Clusterin acts as an extracellular chaperone, safeguarding cells against stress-induced damage caused by precipitates of degraded and misfolded proteins. Clusterin expression, both at the mRNA and protein levels, is subject to upregulation or downregulation in various pathological and clinically relevant conditions. These conditions include cancer, organ regeneration, infection, Alzheimer's disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity, and others.

Recombinant Canine Apolipoprotein-J, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 433 amino acids. It has a molecular weight of 50.6 kDa. The protein is engineered with a His tag fused to the N-terminus. The amino acid sequence of this recombinant Canine Apolipoprotein-J is identical to the sequence corresponding to amino acids 23-445 of the UniProtKB/Swiss-Prot entry P25473. Purification is achieved through proprietary chromatographic techniques.

Sterile Filtered White lyophilized (freeze-dried) powder.

Lyophilized from a solution containing phosphate buffered saline (PBS) at pH 7.5.

Reconstitute the lyophilized pellet in deionized water to a final working concentration of 0.5 mg/ml. Allow for complete dissolution.

Store the lyophilized protein at -20°C. After reconstitution, aliquot the protein to avoid repeated freeze-thaw cycles. Reconstituted protein can be stored at 4°C for a limited period; stability is maintained for at least two weeks at this temperature.

Purity determined by SDS-PAGE is greater than 95%.

CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Glycoprotein 80, Gp80, CLU, Clusterin, Apolipoprotein J, Apo-J.

Escherichia Coli.

MKHHHHHHAS DQAVSDTELQ EMSTEGSKYI NKEIKNALKG VKQIKTLIEQ TNEERKSLLS NLEEAKKKKE DALNDTKDSE TKLKASQGVC NDTMMALWEE CKPCLKQTCM KFYARVCRSG SGLVGHQLEE FLNQSSPFYF WMNGDRIDSL LENDRQQTHA LDVMQDSFNR ASSIMDELFQ DRFFTREPQD TYHYSPFSLF QRRPFFNPKF RIARNIIPFP RFQPLNFHDM FQPFFDMIHQ AQQAMDVNLH RIPYHFPIEF PEEDNRTVCK EIRHNSTGCL KMKDQCEKCQ EILSVDCSSN NPAQVQLRQE LSNSLQIAEK FTKLYDELLQ SYQEKMFNTS SLLKQLNEQF SWVSQLANLT QSEDPFYLQV TTVGSQTSDS NVPVGFTKVV VKLFDSDPIT VMIPEAVSRN NPKFMETVAE KALQEYRQKHREE.