Heat Shock Protein 104 (HSP104)

In response to adverse changes in their environment, cells from many organisms increase the expression of a class of proteins referred to as heat shock or stress proteins. The most well recognized are the Hsp70 and Hsp90 families of proteins. More recently discovered is the Hsp100 (Clp) family of proteins that are highly conserved from eukaryotes to bacteria (which includes yeast, plants, and trypanosomes with the exception of Drosophilia). They share a common function in helping organisms to survive extreme stress. Hsp100 proteins generally have amino acid sequences of about 900 residues and contain two nucleotide binding sites. The two ATP-binding domains of yeast Hsp104 have different functions. One controls the assembly of the protein into a homoligomeric complex and the other controls most of the ATPase activity. Hsp104 of yeast and ClpB of E. coli have significant sequence homology particularly in the two nucleotide binding sites and both of these proteins are required for thermotolerance at extreme temperatures (1,4). Hsp104 can protect yeast cells against high temperature and high concentrations of ethanol but mutation studies have shown this protein is not required for normal growth. The biochemical activities of Hsp100 proteins that allows them to provide thermotolerance are not currently understood. In yeast, Hsp104 has been observed to possess partial functional interchangeability with the Hsp70 family of proteins. This suggests that both protein families may be performing at least some complementary biological function (2). Hsp104 might promote the proteolysis of damaged proteins that are not salvageable by Hsp70, or Hsp104 might serve as another chaperone, binding to damaged proteins and promoting refolding. \n \nApplications: \nWestern Blot (ECL) (3,5): 1:5,000 \nOptimal dilutions to be determined by researcher.

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SPECIFICATIONS

Catalog Number

H1833-01

Size

50ug

Applications

WB

Hosts

Rabbit

Form

Serum

P Type

Pab

Purity

Serum

Isotype

IgG

References

1. Sanchez, Y. and Lindquist, S.L. (1990) Science 248: 1112-1115. \n2. Sanchez, Y., Parsell DA, Taulien J., Vogel J.L., Craig E.A., Lindquist S. (1993) J. \nBacteriology. 175: 6484-6491. \n3. Parsell, D.A., Sanchez, Y., Stitzel, J.D. and Lindquist, S. (1991) Nature 353: 270-273. \n4. Sanchez, Y., Taulien, J., Borkovich, K.A. and Lindquist, S. (1992) The EMBO J. 11: 2357-\n2364. \n5. Ferreira, P.C., Ness, F., Edwards, S.R., Cox, B.S. and Tuite, M.F. (2001) Mol. Microbiol. \n40 (6): 1357-1369. \n

Additional Info

Detects a 104kD protein, corresponding to the apparent molecular mass of Hsp104 on SDS-PAGE immunoblots, in samples from yeast (S. cerevisiae). This antibody also Detects a ~50kD band in yeast samples on immunoblot analysis. No reactivity is detected in immunoblot analysis with human, mouse, rat monkey and hamster proteins.