The Heat Shock 70 kDa Protein (Hsp70) is a member of the heat shock protein family, which plays a crucial role in protein homeostasis. These proteins are highly conserved across different species, indicating their fundamental importance in cellular processes . Hsp70 proteins are involved in various cellular functions, including protein folding, protection against stress, and assisting in the degradation of misfolded proteins .
Hsp70 proteins consist of three major functional domains:
Hsp70 proteins are upregulated in response to various stress conditions, such as heat shock, heavy metals, and toxic chemicals . This upregulation helps protect cells from adverse effects by stabilizing unfolded or misfolded proteins and preventing their aggregation .
The heat shock response was first discovered by Ferruccio Ritossa in the 1960s when a lab worker accidentally increased the incubation temperature of Drosophila (fruit flies). This led to the observation of a “puffing pattern” in the chromosomes, indicating elevated gene transcription of an unknown protein, later identified as heat shock proteins .
The Mouse Anti-Human Hsp70 antibody is a monoclonal antibody that specifically targets the Hsp70 protein in humans. This antibody is widely used in various research applications, including immunohistochemistry, immunoprecipitation, flow cytometry, western blotting, and immunocytochemistry .
The Mouse Anti-Human Hsp70 antibody is suitable for several applications:
The antibody’s specificity and versatility make it a valuable tool for studying the role of Hsp70 in various biological processes and diseases.