Heat Shock Protein 65, Recombinant, Mycobacterium bovis BCG (HSP65)

Hsp65 isolated from Mycobacterium bovis BCG, is a member of the hsp60 family of heat shock proteins (2, 3). Hsp60s are mitochondrial chaperonins that are typically held responsible for the transportation and refolding of proteins from the cytoplasm into the mitochondrial matrix. In addition to its role as a heat shock protein, Hsp60 functions as a chaperonin to assist in folding linear amino acid chains into their respective three-dimensional structure. Hsp60s are a ubiquitous class of HSPs that specifically promote the folding and assembly of cellular polypeptides in an ATP-dependent manner (1). Specifically, sequence comparison of Hsp65 from different mycobacterium strains showed that the protein sequence of M. bovis BCG is identical to that of M. tuberculosis, and very similar to that of M. leprae, the pathogens that cause tuberculosis and tuberculoid leprosy, respectively (2,4). Mycobacterium bovis BCG Hsp65 was identified as the immunodominant antigen during mycobacterial diseases and vaccination. It is also believed to be the antigen that induces autoimmune disease, such as adjuvant arthritis in rats (5, 6). \n\nSource:\nRecombinant Mycobacterium bovis BCG Hsp65 expressed in E.coli.\n\nApplications:\nSuitable for use in Western Blot. Other applications not tested.\n\nRecommended Dilution:\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing.. Store at -20 degrees C. Aliquots are stable for at least 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

H1830-89B

Size

50ug

Applications

WB

Form

Supplied as a liquid in 20mM Tris, 150mM sodium chloride and 10% glycerol.

Purity

~90% (SDS-PAGE).

References

1. Koll H., et al. (1992) Cell 68:1163-1175. 2. Thole J.E.R., et al. (1985) Infect. Immuno. 50:800-806. \n3. Thole J.E.R., et al., (1987) Infect. Immuno. 55:1466-1475. 4. Shinnick T.M. Sweetser D., Thole J., van Embden J. and Young R.A. (1987) Infect. Immuno. 55:1932-1935. 5. Van Eden W., et al. (1988) Nature 331:171-178. 6. Cobelens P.M., et al. (2002) Rheumatology 41:775-779.