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Products >  Protein_Research >  Protein_Folding_and_Expression >  Chaperonin_GroE

Chaperonin GroE

Chaperonin GroE is a protein complex composed of GroEL (14 subunits, 57 kDa) and GroES (7 subunits, 10 kDa). It is thought to support the ability of proteins to form tertiary structure upon (or immediately after) translation. GroE is essential to assembly (and presumably reassembly after denaturation) of protein complexes in vivo. Chaperonin GroEL and GroES can be used for refolding denatured proteins to recover functional activity.
At-A-Glance Documents

Applications

  • Facilitates refolding of denatured proteins

Source

Escherichia coli

Purity

Greater than or equal to 90% on SDS-PAGE.

Storage

–20°C

Properties

GroEL:

  • Molecular weight: (one subunit)
    • 57,000 (amino acid sequence)
    • 60,000 (SDS-PAGE)
  • Isoelectric point: 4.7
  • Optimum pH: 7.0–8.0
  • Stable pH range: 6.0–9.0
  • Optimal temperature: 20–37°C
  • Tolerance to denaturants: stable against <100 mM Guanidine-HCl
  • Thermal stability: stable at <40°C

GroES:

  • Molecular weight:(one subunit)
    • 10,000 (amino acid sequence)
    • 15,000 (SDS-PAGE)
  • Isoelectric point: 5.0
  • Optimum pH: 7.0–8.0
  • Stable pH range: 6.0–9.0
  • Optimal temperature: 20–37°C
  • Tolerance to denaturants: stable against <100 mM Guanidine-HCl
  • Thermal stability: stable at <40°C

Form

Lyophilized (containing the amount equivalent to 200 µL of 5mM Tris-HCl buffer, pH 7.8)

References

  1. Martin, J. et al. (1991) Nature, 352, 36-42.
  2. Viitanen, P.V. et al. (1991) Biochemistry, 30, 9716-9723.
  3. Laminet. A. et al. (1989) EMBO J. 8:1469-77.
  4. Mendoza, J.A. et al. (1991) J. Biol. Chem., 266, 13044-13049.
  5. Rosenberg, H. F. et al. (1993) J. Biol. Chem. 268:4499-503.
  6. Brandsch, R. et al. (1992) J. Biol. Chem., 267, 20844-20849.
  7. Schmidt, M. et al. (1992) J. Biol. Chem., 267, 16829-16833.
  8. Holl-Neugebauer, B. et al. (1991) Biochemistry, 30, 11609-11614.
  9. Battistoni, A. et al. (1993) FEBS Letters 322:6-9.
  10. Buchner, J. et al. (1991) Biochemistry, 30, 1586-1591.
  11. Kern, G. et al. (1992) FEBS Letters, 305, 203-205.
  12. Badcoe, I.G. et al. (1991) Biochemistry, 30, 9195-9200.
  13. Hartman, D.J. et al. (1993) Proc. Natl. Acad. Sci. USA, 90, 2276-2280.
  14. Escher, A. et al. (1993) Mol. Genet., 238, 65-73.
  15. Kubo, T. et al. (1993) J. Biol. Chem. 268:19346-51.
  16. Goloubinoff, P. et al. (1989) Nature 342:884-9.
  17. Viitanen, P.V. et al. (1990) Biochemistry, 29, 5665-5671.
  18. van der Vies, S. M. et al. (1992) Biochemistry, 31, 3635-3644.
  19. Goloubinoff, P. et al (1989) Nature, 377, 44-47.
  20. Grimm, R. et al. (1993) J. Biol. Chem., 268, 5220-5226.
  21. Zheng, X. et al. (1993) J. Biol. Chem. 268:7489-93.
  22. Brunschier, R. et al. (1993) J. Biol. Chem., 268, 2767-2772.
  23. Wynn, R. M. et al. (1992) J. Biol. Chem., 267, 12400-12403.
  24. Mizobata, T. et al. (1992) J. Biol. Chem. 267:17773-9.
  25. Fisher, M. T. (1992) Biochemistry 31:3955-63.



 
 
Products
Cat. # Product Package Size Price # of Units Select
7330 Chaperonin Gro EL 5 mg $232.00
7331 Chaperonin Gro ES 0.5 mg $232.00
 

 


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