HSP65 Protein

CAT: 0400-SPR-116ASize: 50 µgDry Ice: NoHazardous: No
CAT#:0400-SPR-116ASize:50 µg
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24/48H Stock Items & 2 to 6 Weeks non Stock Items.
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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
Product MSDS
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