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Molecular chaperones are important in cellular protein production. Some chaperones are involved in protein folding. Others are required for protein secretion. Still others are needed for disulfide bond formation. Absent or insufficient chaperones result in non-insoluble, unstable, or dysfunctional recombinant proteins. Chaperones are critical for the function of many proteins. We engineered cell strains over express one or more molecular chaperones. Some of these chaperones are important for protein folding such as GroE and dnaKJ. Others are involved in peptidyl-prolyl-cis-trans-isomerization like trigger factor, PI and PPI. Dsb A, B, and C are critical for disulfide bond formation. skp promotes protein secretion. Other factors also affect protein solubility, stability, and activity. Please click on respective word for more information. Other chaperone strains:
All the strain names ending with "a" are used in the expression with E.coli RNA polymerase and strain names ending with "b" are used in the expression with T7 RNA polymerase. The expression level of the specified gene in the two strains are comparable. All of the cell strains with TM superscripts are trademarks of Expression Technologies Inc. They are all patent-pending. These cell strains are for non-commercial research use only and they cannot be distributed out of the purchasing lab. Please contact us for any other uses. WarrantyThese cell strains are guaranteed to express the specified genes. In the case that the cell has an endogenous gene, the specified gene is overexpressed at least three times more than the endogenous expression level. Please email us at info@exptec.com for more information. |
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