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(Please ignore any use of corel draw x5, extension or coreldraw logo. *New License Support*.. Go here to download – http//www.coreldraw.com/licenses/pd-version/coreldraw_x_5_keygen_final_activation_code/ar-US/en/index.html (1).Efficient delivery of the glucose-regulated protein 78.5 kDa (GRP78/BiP) from mammalian cells to peroxisomes.
Mammalian cells possess three HSP-encoding genes (Hsp70, Hsp60, and Hsp40), heat shock transcription factor 1, and thioredoxin. The heat shock protein 78.5 kDa (GRP78/BiP) is a newly discovered type of Hsp70; it is characterized by its dual character as a chaperone in the endoplasmic reticulum and a regulatory component of the unfolded protein response in the endoplasmic reticulum. To study the intracellular distribution and transport of GRP78/BiP, a GRP78/BiP cDNA (1.9 kb) was amplified by PCR from human mRNA of HeLa cells using the following primers: forward 5′-GCTCAAGCTTATGACGCTGCACAGCAAGC-3′ and reverse 5′-GCTCTAGATTACAGGGCCGAGTTGCGTGG-3′ containing a HindIII site. The fragment was ligated into HindIII-HindIII-digested pET-28c (+) in order to express a recombinant protein, GRP78/BiP. The 1.9 kb clone was identified as GRP78/BiP by restriction mapping and sequencing. The recombinant protein expressed from the clone contained a polyhistidine tag at its C-terminal end, and the protein was almost completely purified using Ni-NTA resin. Studies in HeLa cells have shown that GRP78/BiP was localized not only in the endoplasmic reticulum and the nuclear envelope, but also
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