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Products >  Protein_Research >  Protein_Folding_and_Expression >  Chaperonin_GroE

Chaperonin GroE

Chaperonin GroE is a 21mer protein complex composed of the subunits GroEL (14mer, 57 kDa) and GroES (7mer, 10 kDa). This complex is thought to support the protein expression and folding ability, enabling proteins to form tertiary structures upon (or immediately after) translation. Chaperonin GroE is essential to the assembly (and presumably reassembly after denaturation) of protein complexes in vivo. Both chaperonin GroEL and GroES can be used for refolding denatured proteins to recover functional activity.
At-A-Glance Documents Images & Data

Applications

  • Protein expression and folding
  • Refolding 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 kDa (amino acid sequence)
    • 60 kDa (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 kDa (amino acid sequence)
    • 15 kDa (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 (contains an 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. 8:1469-1477.
  4. Mendoza, J.A. et al. (1991) J. Biol. Chem. 266:13044-13049.
  5. Rosenberg, H. F. et al. (1993) J. Biol. Chem. 268:4499-4503.
  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. 268:19346-19351.
  16. Goloubinoff, P. et al. (1989) Nature 342:884-889.
  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. 268:7489-7493.
  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. 267:17773-17779.
  25. Fisher, M. T. (1992) Biochemistry 31:3955-3963.



 
 
Products
Cat. # Product Package Size Price # of Units Select
7330 Chaperonin Gro EL 5 mg $237.00
7331 Chaperonin Gro ES 0.5 mg $237.00
 

 


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