ST13 Antibody

Heat Shock Protein 70 (HSP70) is a highly conserved protein family that plays a crucial role in protein homeostasis. HSP70 proteins are molecular chaperones that assist in the folding of nascent proteins, the refolding of misfolded or aggregated proteins, and the transport of proteins across cellular membranes. The interaction of HSP70 with various client proteins and co-chaperones is essential for its function. This article delves into the background of HSP70 interacting proteins, focusing on the mouse anti-human HSP70 antibody.

The HSP70 family is one of the most conserved protein families across all eukaryotes. Members of this family are induced by various stress conditions, including heat shock, oxidative stress, and exposure to toxins. HSP70 proteins are involved in numerous cellular processes, including protein folding, protection against stress-induced damage, and the regulation of protein degradation pathways .

HSP70 interacts with a wide range of client proteins and co-chaperones. These interactions are critical for the protein’s chaperone activity. The binding of HSP70 to its client proteins is mediated by its substrate-binding domain, while the nucleotide-binding domain regulates the binding and release of substrates. Co-chaperones, such as HSP40, assist HSP70 in recognizing and binding to client proteins .

Recent studies have employed advanced techniques like cross-linking mass spectrometry (XL-MS) to comprehensively characterize the HSP70 interactome. These studies have identified numerous novel client proteins and interactions mediated by posttranslational modifications (PTMs). PTMs play a significant role in regulating the function of client proteins by facilitating their interaction with HSP70 .

The mouse anti-human HSP70 antibody is a monoclonal antibody that specifically recognizes the HSP70 protein in human cells. This antibody is widely used in research to study the expression and function of HSP70 in various biological contexts. It is particularly useful in techniques such as Western blotting, immunoprecipitation, and immunofluorescence .

The mouse anti-human HSP70 antibody has been instrumental in advancing our understanding of HSP70’s role in cellular processes. For instance, it has been used to investigate the anti-inflammatory mechanisms of HSP70, where endogenous HSP70 was found to protect against induced colitis in mice . Additionally, this antibody has been employed in studies exploring the role of HSP70 in cancer, neurodegenerative diseases, and viral infections .