HSP65 Protein

• Background :

  HSP65, a member of the HSP60 family, is a mitochondrial chaperonin originally identified in Mycobacterium bovis BCG. It shares high sequence homology with HSP60 proteins across species and plays a central role in protein folding, particularly in the mitochondrial matrix. Like other chaperonins, HSP65 assists in the ATP-dependent folding and assembly of polypeptides, ensuring proper protein conformation and cellular function. While HSP65 is most commonly studied in the context of infectious disease and immunology—particularly as an immunodominant antigen in tuberculosis and leprosy—its structural and functional similarity to mammalian HSP60 has drawn attention in neurodegenerative disease research. Mitochondrial dysfunction and impaired proteostasis are key features of neurodegenerative disorders such as Alzheimer’s, Parkinson’s, and multiple sclerosis. Given its chaperone activity, HSP65 serves as a model for understanding mitochondrial stress responses and protein misfolding in neurons. Moreover, HSP65 has been implicated in autoimmune responses, including experimental models of neuroinflammation. Its ability to trigger immune activation and molecular mimicry may contribute to the development of neuroimmune disorders, offering insights into the intersection of infection, immunity, and neurodegeneration. As a result, HSP65 is increasingly recognized not only as a microbial antigen but also as a valuable tool for studying mitochondrial resilience, neuroinflammation, and protein misfolding in the context of neurodegenerative disease.

• Description :

  Mycobacterium bovis BCG Recombinant HSP65 Protein

• Product Name Alternative :

  60kDa chaperonin 2, Antigen A, Cell wall A, groEL, GroEL2, GroL2, M. Tuberculosis cell wall A, M. Tuberculosis HSP65, Cpm60 2

• UNSPSC :

  12352202

• UN Code :

  Non-hazardous

• Hazard Statement :

  Non-hazardous

• Swiss Prot :

  P0A521

• Accession Number :

  M17705.1

• Cellular Locus :

  Cytoplasm

• Expression System :

  E. coli

• Host :

  E. coli

• Origin Species :

  Bacteria

• Target :

  HSP65

• Conjugation :

  No tag

• Nature :

  Recombinant

• Sequence :

  MAKTIAYDEEARRGLERGLNALADAVKVTLGPKGRNVVLEKKWG APTITNDGVSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVREG LRNVAAGANPLGLKRGIEKAVEKVTETLLKGAKEVETKEQIAATAAISAGDQSIGDLI AEAMDKVGNEGVITVEESNTFGLQLELTEGMRFDKGYISGYFVTDPERQEAVLEDPYI LLVSSKVSTVKDLLPLLEKVIGAGKPLLIIAEDVEGEALSTLVVNKIRGTFKSVAVKA PGFGDRRKAMLQDMAILTGGQVISEEVGLTLENADLSLLGKARKVVVTKDETTIVEGA GDTDAIAGRVAQIRQEIENSDSDYDREKLQERLAKLAGGVAVIKAGAATEVELKERKH RIEDAVRNAKAAVEEGIVAGGGVTLLQAAPTLDELKLEGDEATGANIVKVALEAPLKQ IAFNSGLEPGVVAEKVRNLPAGHGLNAQTGVYEDLLAAGVADPVKVTRSALQNAASIA GLFLTTEAVVADKPEKEKASVPGGGDMGGMDF

• Applications :

  WB | SDS-PAGE | Functional Assay | ELISA

• Field of Research :

  Cancer | Heat Shock

• Purification Method :

  Multi-Step Purified

• Purification :

  Multi-Step Purified

• Limit Of Detection :

  This product has been certified >90% pure using SDS-PAGE analysis.

• Concentration :

  Lot/batch specific. See included datasheet.

• Purity :

  >90%

• Weight :

  0.05

• Length :

  Full Length

• Buffer :

  20mM Tris/HCl, pH 7.5, 0.45M NaCl, 10% glycerol, 5mM bMe

• Molecular Weight :

  ~65 kDa

• Precautions :

  Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.

• References & Citations :

  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.

• Shipping Conditions :

  Blue Ice or 4ºC

• Storage Conditions :

  -20ºC

• Protein Length :

  Full Length

• Background Reference 01 :

  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.

• Location :

  Cytoplasm

• AA Sequence :

  MAKTIAYDEEARRGLERGLNALADAVKVTLGPKGRNVVLEKKWG APTITNDGVSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVREG LRNVAAGANPLGLKRGIEKAVEKVTETLLKGAKEVETKEQIAATAAISAGDQSIGDLI AEAMDKVGNEGVITVEESNTFGLQLELTEGMRFDKGYISGYFVTDPERQEAVLEDPYI LLVSSKVSTVKDLLPLLEKVIGAGKPLLIIAEDVEGEALSTLVVNKIRGTFKSVAVKA PGFGDRRKAMLQDMAILTGGQVISEEVGLTLENADLSLLGKARKVVVTKDETTIVEGA GDTDAIAGRVAQIRQEIENSDSDYDREKLQERLAKLAGGVAVIKAGAATEVELKERKH RIEDAVRNAKAAVEEGIVAGGGVTLLQAAPTLDELKLEGDEATGANIVKVALEAPLKQ IAFNSGLEPGVVAEKVRNLPAGHGLNAQTGVYEDLLAAGVADPVKVTRSALQNAASIA GLFLTTEAVVADKPEKEKASVPGGGDMGGMDF

• Immunogen Species :

  Bacteria