HSP65 Protein

Mycobacterium bovis BCG Recombinant HSP65 Protein

Product Specifications

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.

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

0.1

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.