Hyperstable Hsp60 (Pf Cpn) Protein

This hyperstable chaperonin Hsp60 (Pf Cpn) from Pyrococcus furiosus was recombinantly produced in E. coli and posesses non-native protein salvage activity including ability to deconstruct amyloid fibrils (prions).

Pyrococcus furiosus is an hyperthermophilic species of Archaea. It is notable for having an optimum growth temperature of 100C. Hyperstable Hsp60 (Pf Cpn) Protein acts as a chaperone to enhance protein folding and increase enzyme or microbial resistance to heat. Dr. Robb found that the thermostability of Taq polymerase was significantly improved by combinations of P. furiosus chaperones, showing ongoing protein folding activity at elevated temperatures and during thermal cycling. These properties may be exploited to enhance the durability and cost effectiveness of high temperature biocatalysts.

From the laboratory of Frank T. Robb, PhD, University of Maryland, Baltimore, Institute of Marine and Environmental Technology (IMET).

Catalog Number Product Size AVAILABILITY Price Qty
Hyperstable Hsp60 (Pf Cpn) Protein
25ug In stock
Regular Price:$256.00

Product Type: Protein
Name: HSP60, Pf Cpn
Accession ID: PFC_08710 (JGI)
Source: E. coli BL21
Molecular Weight: 60 kDa
Purity: 100
Buffer: HEPES 50 mM, pH7.5
Concentration: 1 mg/mL
Activity: ug/min/mg ATPase
Suggested Amount per Experiment: 50 ng
Comments: Hyperstable. Hexadecamer, 1mDa complex
Storage: -80C
Shipped: Dry Ice


Purity Analysis of Recombinant Pf Cpn.

The recombinant Pf Cpn was analyzed by SDS–PAGE (5 ug) and 6% Native gel (20 ug). The native gel markers from top to bottom are IgM Hexamer, 1236 kDa; IgM Pentamer, 1048 kDa; Apoferritin band 1, 720 kDa; Aproferritin band 2, 480 kDa; and B-phycoerythrin, 242 kDa.

Adapted from: Luo H, et al. (2009) Arch Biochem Biophys. 486:12-18.

From the laboratory of Frank T. Robb, PhD, University of Maryland, Baltimore, Institute of Marine and Environmental Technology (IMET)
  1. Sun, Y., N. Makarava, C-I. Lee, P. Laksanalamai, F. T. Robb and I. V. Baskakov (2008) Conformational stability of PrP amyloid fibrils controls their smallest possible fragment size. J. Molecular Biology 376(4):1155 - 1167.
  2. Luo H, Laksanalamai P, Robb FT. (2009) An exceptionally stable Group II chaperonin from the hyperthermophile Pyrococcus furiosus. Arch Biochem Biophys. 486:12-18.
  3. Kurouski D, Luo H, Sereda V, Robb FT, Lednev IK (2013) Deconstruction of stable cross-Beta fibrillar structures into toxic and nontoxic products using a mutated archaeal chaperonin. ACS Chem Biol. 2013 Sep 20;8(9):2095-101. doi: 10.1021/cb400238

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