The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation via its oxidase activity and isomerization via its isomerase activity, as well as the reduction of disulphide bonds in proteins (1). Studies suggest BiP and PDI work together sequentially to increase oxidation of these proteins (2, 3). PDI has also been found to function as a chaperone to prevent the aggregation of unfolded substrates, and serves as a subunit of prolyl 4-hydroxylase and microsomal triglyceride transferase (4, 5).nPDI is an abundant 55kDa protein located primarily in the ER, however studies have also proved its presence in the cytosol (1). PDI has the ability to reside in the ER permanently due to the highly conserved KDEL sequence at its carboxy-terminus (6). It uses carboxy-terminal KDEL as a retention signal, and this appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor (7).
StressMarq Biosciences Inc. 在2007年成立于加拿大維多利亞,是一家生物科技公司,專門從事試劑與試劑盒研究,服務范圍遍及2400多個國家。 StressMarq公司的核心技術領域為細胞應激(尤其是熱休克蛋白(HSP)領域,領先全球),離子通道,載體研究,同時在神經(jīng)科學領域推出特有的具有生物活性的Tau蛋白與A-突觸核蛋白。產(chǎn)品領域涉及到:細胞凋亡、細胞信號、通路和轉運、細胞器標志物、熱休克、神經(jīng)生物學、神經(jīng)科學、氧化應激、磷酸化運輸?shù)取3颂峁┯糜谶M一步研究的相關工具外,Str