Heat shock proteins (HSPs) are a family of proteins that play a crucial role in protecting cells from stress. Among them, Heat Shock Protein 90-alpha (HSP90α) is a highly conserved molecular chaperone involved in the proper folding, stabilization, and degradation of many proteins. This article delves into the background of HSP90α, particularly focusing on the mouse anti-human HSP90α antibody.
HSP90α is one of the isoforms of the HSP90 family, which also includes HSP90β. It is a cytosolic protein that is highly expressed in eukaryotic cells and accounts for 1-2% of total cellular proteins under non-stressed conditions. This percentage can increase to 4-6% under stress conditions .
HSP90α is composed of three main domains:
The primary function of HSP90α is to act as a molecular chaperone, assisting in the proper folding of nascent proteins, stabilization of proteins against heat stress, and aiding in protein degradation. It also plays a significant role in the maturation and activation of various client proteins, including steroid hormone receptors, kinases, and transcription factors .
HSP90α is implicated in various diseases, particularly cancer. It stabilizes several oncoproteins, making it a target for anti-cancer therapies. HSP90 inhibitors are being investigated for their potential to disrupt the function of HSP90α, thereby destabilizing its client proteins and inhibiting tumor growth .
Mouse anti-human HSP90α antibodies are monoclonal or polyclonal antibodies developed in mice to specifically target the human HSP90α protein. These antibodies are widely used in research and diagnostic applications, including Western blotting, immunoprecipitation, immunohistochemistry, and flow cytometry .
The development of mouse anti-human HSP90α antibodies involves immunizing mice with human HSP90α protein or peptides, followed by the collection and purification of the antibodies produced. These antibodies are then validated for their specificity and reactivity with human HSP90α .
In research, these antibodies are used to study the expression, localization, and function of HSP90α in various biological contexts. They are also employed in diagnostic assays to detect HSP90α levels in clinical samples, aiding in the diagnosis and prognosis of diseases such as cancer .