Glucose Regulated Protein E (GrpE)

GrpE is an acidic 24 kD protein encoded by a monocistronic Escherichia coli gene (located at 56 min.) which is under the control of both s32 and s70 transcription factors. The GrpE protein functions as a co-chaperone in assisting the DnaK (Hsp70) protein to effectively carry out DnaK-dependent chaperone activity (i.e., protein folding, protein transport, disaggregation of heat inactivated proteins, activation of mutant proteins). DnaK and DnaJ assist protein folding by\nstabilizing an intermediate conformation; where as the GrpE protein, in an ATP-dependent reaction, releases partially folded protein from the DnaK/J complex and transfers this immature protein to the GroEL/ES chaperone complex to finish the protein folding reaction2. GrpE co-chaperone protein assists the DnaK chaperone during two crucial steps: binding to protein substrate and releasing DnaK chaperone from the complex with substrate. In the first case, the\npresence of GrpE protein releases those substrates not tagged by the DnaJ protein from DnaK complexes. In this case, GrpE protein works as a discrimination factor. In the second step, GrpE and DnaJ proteins jointly accelerate DnaK

Prices direct from United States Biological

Quick response times

Exclusive Biosave savings/discounts

SPECIFICATIONS

Catalog Number

G3057-63

Size

200ug

Applications

WB

Hosts

Rabbit

Form

Supplied as a liquid in TBS, pH 7.5, 0.1% sodium azide, 50% glycerol.

P Type

Pab

Purity

Purified by Protein A affinity chromatography.

Isotype

IgG

References

1. Zylicz, M., Ang, D. and Georgopoulos, C. (1987) J. Biol. Chem. 262: 17437-17442. 2. Bang, H., Pecht, A., Raddatz, G., Scior, T., Solbach, W., Brune, K. and Pahl, A. (2000) Eur. J. Biochem. 267: 3270-3280. 3. Langer, T., et. al. (1992) Nature 365: 683-689

Additional Info

Recognizes E. coli GrpE. Detects a 24kD protein, corresponding to the apparent molecular mass of GrpE on SDS-PAGE immunoblots, in samples from E. coli. Does not react with proteins from human, mouse, rat nor yeast lysates.