Chaperon Proteins and Disullfide Bond Isomerase

Chaperon Proteins and Disullfide Bond Isomerase

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DnaK (HSP70) E. Coli Recombinant
DH5aTM is the most frequently used E.Coli strain for routine cloning applications. In addition to supporting blue/white screening recA1 and endA1 mutations in DH5a increase insert stability and improve the quality of plasmid DNA prepared from minipreps.
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GroEL
GroEL protein is a member of the chaperonin family that is required for proper protein folding. GroEL consists of 14 subunits with a total molecular weight of 57.3kDA. The recombinant full length protein was overexpressed in E.coli and purified by chromatography.
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GroES
GroES protein is a chaperonin family protein that works in conjunction with GroEL to facilitate proper protein folding. GroES consists of 7 subunits with a molecular weight of 10.4kDA. The recombinant full length protein was overexpression in E.coli and purified by chromatography.
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PDI1 (yeast)
Recombinant yeast PDI is produced in E.Coli is as single, non-glycosylated, polypeptide chain containing 503 amino acids and having a molecular mass of 62.4 kDa. The PDI is fused to a 12 amino acid His tag (515 a.a. total) at N-terminal and purified by proprietary chromatographic techniques.
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