CDC37(Phospho-Ser13) Rabbit Polyclonal Antibody

The protein encoded by this gene is highly similar to Cdc 37| a cell division cycle control protein of Sacchromyces cerevisiae. This protein is a molecular chaperone with specific function in cell signal transduction. It has been shown to form complex with Hsp90 and a variety of protein kinases including CDK4| CDK6| SRC| RAF-1| MOK| as well as eIF2 alpha kinases. It is thought to play a critical role in directing Hsp90 to its target kinases.

The CDC37(Phospho-Ser13) Rabbit Polyclonal Antibody is a highly specific and sensitive tool designed for the detection and analysis of CDC37 protein phosphorylated at Serine 13. This antibody is produced using high-quality rabbit polyclonal antibodies, ensuring reliable and reproducible results.

CDC37 is a crucial co-chaperone protein that plays a vital role in the regulation of protein folding and stability. Phosphorylation of CDC37 at Serine 13 has been implicated in various cellular processes, including cell cycle progression, protein kinase signaling, and oncogenesis. Therefore, the ability to accurately detect and quantify phosphorylated CDC37 at Serine 13 is of utmost importance in understanding the underlying mechanisms of these processes.

The CDC37(Phospho-Ser13) Rabbit Polyclonal Antibody exhibits exceptional specificity and sensitivity, enabling precise detection of phosphorylated CDC37 at Serine 13 in various sample types, including cell lysates and tissue extracts. This antibody has been extensively validated through rigorous testing, ensuring its reliability and accuracy.

Furthermore, the CDC37(Phospho-Ser13) Rabbit Polyclonal Antibody is compatible with a wide range of applications, including Western blotting, immunoprecipitation, and immunofluorescence. Its versatility allows for comprehensive analysis of phosphorylated CDC37 at Serine 13 in different experimental settings.

In summary, the CDC37(Phospho-Ser13) Rabbit Polyclonal Antibody is a valuable tool for researchers studying the role of CDC37 phosphorylation in various cellular processes. Its high specificity, sensitivity, and compatibility with multiple applications make it an essential component in elucidating the intricate mechanisms underlying protein folding, stability, and signaling pathways.