GroEL antibody is a molecular tool used to detect and study the GroEL chaperonin, a 60 kDa protein critical for protein folding and cellular stress responses. It is a member of the heat shock protein 60 (HSP60) family and functions as part of the GroE system (GroEL-GroES) in bacteria, aiding in the refolding of partially unfolded proteins and preventing aggregation . The antibody is employed in research to analyze GroEL’s role in protein homeostasis, bacterial pathogenesis, and immune responses.
GroEL forms a double toroidal structure with 14 identical subunits arranged into two stacked heptameric rings, creating a cavity for substrate binding . Key functions include:
Protein Folding: Facilitates ATP-dependent refolding of nascent or misfolded proteins by providing a hydrophilic environment in its nanochamber .
Aggregation Prevention: Captures transient hydrophobic patches on partially folded proteins, preventing aggregation during stress conditions .
Immune Modulation: Acts as a surface-exposed antigen in pathogens like Cronobacter sakazakii and Rickettsia, triggering host immune responses .
GroEL antibodies enable precise detection and functional analysis of GroEL across diverse contexts:
9A1/2: Widely used for E. coli GroEL detection, validated in Western blot (1:10,000 dilution) .
P2E4AT: Targets human GroEL, useful in studying HSP60-related diseases .
ProSpec Bio: Cross-reacts with bacterial GroEL, applied in immunohistochemistry (1:50–100 dilution) .
GroEL antibodies are pivotal in understanding bacterial pathogenesis and host-pathogen interactions:
Bacterial Virulence: C. sakazakii GroEL enhances adhesion to host cells, induces cytokine release (TNF-α, IL-6), and disrupts epithelial barriers .
Diagnostic Tools: Monoclonal antibodies like BNI52 enable specific detection of Rickettsia spp. in infected cell cultures or patient sera .
Therapeutic Potential: Targeting GroEL may mitigate bacterial aggregation and biofilm formation, though clinical applications remain under investigation .
GroEL, also known as Heat Shock Protein 60 (HSP60), is a molecular chaperonin that plays a crucial role in protein folding and maintaining cellular homeostasis. It is highly conserved across different species, from prokaryotes to eukaryotes. In prokaryotes, GroEL functions as part of the GroEL/GroES complex, which forms a double-ring structure that assists in the proper folding of proteins .
GroEL is a 60 kDa protein that forms a complex with GroES, another chaperonin, to create a functional unit essential for protein folding. This complex operates by encapsulating unfolded or misfolded proteins within its central cavity, providing an isolated environment where proteins can achieve their correct conformation. This process is ATP-dependent and involves multiple cycles of binding and release .
In eukaryotes, HSP60 is located in the mitochondria and is involved in the folding of mitochondrial proteins. It also plays a role in protecting cells from stress by preventing the aggregation of misfolded proteins. HSP60 is implicated in various cellular processes, including apoptosis, oxidative stress response, and immune response .
HSP60 has been studied extensively for its role in various diseases. It is considered a potential therapeutic target for conditions such as cancer, neurodegenerative diseases, and inflammatory disorders. The protein’s involvement in maintaining mitochondrial integrity and its role in apoptosis make it a critical factor in cell survival and disease progression .
The mouse anti-human GroEL (HSP60) antibody is a monoclonal antibody that specifically targets the human HSP60 protein. This antibody is used in various research applications, including Western blotting, immunohistochemistry, and immunofluorescence. It is particularly useful in distinguishing human HSP60 from its bacterial and other mammalian homologs .
The antibody is produced by immunizing mice with recombinant human HSP60 protein, leading to the generation of a specific immune response. The resulting monoclonal antibody is then purified and characterized for its specificity and affinity towards human HSP60 .
The mouse anti-human GroEL (HSP60) antibody is widely used in research to study the expression and localization of HSP60 in different tissues and under various conditions. It helps in understanding the role of HSP60 in disease mechanisms and can be used to explore potential therapeutic interventions. For example, in cancer research, this antibody can be used to investigate the expression levels of HSP60 in tumor tissues, providing insights into the protein’s role in tumorigenesis and potential as a therapeutic target .