ELISA Kits - Cellular Stress, Heat Shock Proteins (HSP), Oxidative Stress

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Product Name: Hsp65 StressXpress® ELISA Kit
Catalog #: SKT-113-480
Alternative Names: 60kDa chaperonin 2, Antigen A, Cell wall protein A, groEL, GroEL2, GroL2, M. Tuberculosis cell wall protein A, M. Tuberculosis Hsp65, Protein Cpm60 2
Size: 5 x 96-well
Type: ELISA
Description: ELISA kit used to quantitate the Hsp65 concentration in samples
Species Reactivity: Mycobacterium Bovis Hsp65;Mycobacterium Tuberculosum Hsp65
Sample Type: Cell lysates, tissue extracts, serum samples
Research Area: Chaperones, Heat Shock
Incubation Time: 30 minutes
Sensitivity: 0.06 ng/mL
Assay Range: 0.34-22ng/ml
Storage Temp: 4°C
Shipping Temp: Blue Ice, 4°C
Price: $2,180.00 USD Add to Cart Bulk Quote

Hsp65 ELISA Kit Catalog # SKT-106 (96 well kit)	Download .pdf
Hsp65 ELISA Kit Catalog # SKT-113 MSDS	Download .pdf

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 threedimensional 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. HThole 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. Hinnick T.M. Sweetser D., Thole J., van Embden J., 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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