Product Description

Recombinant E. coli Thiol Disulfide Interchange Protein DsbE is a protein that plays a significant role in the oxidative folding of proteins in the periplasmic space of Escherichia coli bacteria. Belonging to the family of thiol-disulfide oxidoreductases, DsbE facilitates the formation and rearrangement of disulfide bonds, contributing to the correct folding and stability of various proteins. With a molecular weight of approximately 20 kDa, this protein serves as an important component in the cellular machinery involved in protein folding and quality control.

Current Lead Time

7-14 Days

Product Specifications

*For Research Use Only

If your product is within its expiration period, and has not performed according to expectations, fill out the sample return form. Return the unused sample frozen, with the auto generated packing slip to the address on the instructions. You will receive a full refund along with a replacement of the unused portion (inclusive of the failed test). Damages do not cover any additional costs incurred for failed experimentation. 

MRNAEGDDPT NLESALIGKP VPKFRLESLD NPGQFYQADV LTQGKPVLLN VWATWCPTCR AEHQYLNQLS AQGIRVVGMN YKDDRQKAIS WLKELGNPYA LSLFDGDGML GLDLGVYGAP ETFLIDGNGI IRYRHAGDLN PRVWEEEIKP LWEKYSKEAA Q.

Reconstituted store at -20°C or -80°C.We recommend that single use aliquots are prepared to avoid freeze-thaw cycles.

1. Thaw the vial on ice, spin briefly
2. Prepare single-use or stock aliquots. This stage will depend on your final application so please adapt as appropriate. All our proteins are supplied carrier protein-free. If compatible with your work and you are storing at lower concentrations (<50 ug/ml) adding carrier protein is highly advised (usually 1% w/v high purity BSA or equivalent – ensure all buffers are sterile-filtered).
3. Prepare single-use aliquots whenever possible to avoid freeze-thaw cycles which can damage the proteins and reduce bioactivity. Store aliquots at -70 °C (or -20 °C)
4. We recommend sterile filtering after dilution in media or the final working solution
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Not Available