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Product Name: Hsp65 (Recombinant, Mycobacterium Bovis BCG, Native sequence)
Catalog #: SPR-116A
Alternative Names: 60kD chaperonin 2, Antigen A, Cell wall protein A, groEL, GroEL2, GroL2, M. Tuberculosis cell wall protein A, M. Tuberculosis Hsp65, Protein Cpm60 2
Type: Recombinant Protein
Accession Number: M15467
Gene ID: 1091466
SwissProt: P0A520
Applications: WB Control
Species: Mycobacterium bovis BCG
Conjugate/Tag: No tags
Form: Multi-Step Chromatography
Storage Buffer: 20mM Tris, 150mM NaCl and 10% glycerol.
Concentration: 0.5mg/mL
Certificate of Analysis: This product has been certified >90% pure using SDS-PAGE analysis.
Background Info: Molecular weight of approximately 65kD
Package Size: 50ug
Other Information: Native sequence
Storage Temp: -20°C
Shipping Temp: Dry ice, Blue Ice or 4°C
Datasheet: SPR 116 Heat Shock Protein 65 (Hsp65)
Research Area: Heat Shock
Price: $209.00 USD Add to Cart Bulk Quote

SDS PAGE of M. Bovis Hsp65 protein.

Research Background: 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).
References: 1. Koll H., et al. (1992) Cell 68: 1163-1175.
2. Thole J.E.R., et al. (1985) Infect. Immuno. 50: 800- 806.
3. 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.

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