Description

Product name: Poly(ethylene terephthalate) hydrolase (PETase)

Product description: Recombinant PETase from Ideonella sakaiensis (strain 201-F6)1 produced in Nicotiana benthamiana by Agrobacterium-mediated transient expression.

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Description

Host species: Nicotiana benthamiana
Native organism of product: Ideonella sakaiensis (strain 201-F6)

Molecular weight: 28 kDa

Tag: C-terminal His-tag

Uses: For research use only. Examples include SDS-PAGE, Western Blot, functional assays.

Relevance: PETase has been shown to be involved in the first depolymerization step of poly(ethylene terephthalate) (PET). PETase hydrolyses Poly(ethylene terephthalate) to mono(2-hydroxyethyl) terephthalate (MHET). PETase, and its corresponding pathway partner, MHETase (which carries out the second depolymerization step) are of biotechnological interest in the recycling of plastic products into benign materials.2-3

Specification
Please see COA for specific batch number.

Purity: >99 % as shown by SDS-PAGE.

Figure 1: reducing 4-20% SDS-PAGE analysis of 5 µg PETase

Concentration: 1.6 mg/ml (analyzed by A280 measurement)

Aliquot size: 1 x 300 µg per tube

Biological activity: N/A

Endotoxin: Not tested.

Formulation: 20 mM HEPEs, 150 mM NaCl, pH 7.5

Storage

Shipped: Recombinant proteins are sterile-filtered and provided as lyophilized powder which are shipped at ambient temperature.

Stability & Storage: See COA for detailed storage instructions. Lyophilized materials are stable for up to twelve months from the date of receipt at -70℃.

It is recommended that reconstituted protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

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References:
1. https://www.uniprot.org/uniprot/A0A0K8P6T7
2. Yoshida, S. et al, A bacterium that degrades and assimilates poly(ethylene terephthalate) Science, 2016: Vol. 351, Issue 6278, pp. 1196-1199, DOI: 10.1126/science.aad6359
3. Joo, S., Cho, I.J., Seo, H. et al. Structural insight into molecular mechanism of poly(ethylene terephthalate) degradation. Nat Commun 9, 382 (2018) doi:10.1038/s41467-018-02881-1