NBK(Phospho Thr33) Polyclonal Antibody

The protein encoded by this gene shares a critical BH3 domain with other death-promoting proteins, such as BID, BAK, BAD and BAX, that is required for its pro-apoptotic activity, and for interaction with anti-apoptotic members of the BCL2 family, and viral survival-promoting proteins. Since the activity of this protein is suppressed in the presence of survival-promoting proteins, it is suggested as a likely target for anti-apoptotic proteins.

The NBK(Phospho Thr33) Polyclonal Antibody is a highly specific and sensitive tool designed for the detection and quantification of phosphorylated threonine residue at position 33 in various proteins. This antibody has been meticulously developed and rigorously validated to ensure its reliability and accuracy in experimental applications.

With its exceptional affinity and selectivity, the NBK(Phospho Thr33) Polyclonal Antibody offers researchers a valuable tool for investigating the role of phosphorylation at Thr33 in protein function and cellular signaling pathways. It enables the precise identification and characterization of phosphorylated proteins, facilitating a deeper understanding of their biological functions and regulatory mechanisms.

The NBK(Phospho Thr33) Polyclonal Antibody exhibits excellent performance in a wide range of applications, including Western blotting, immunoprecipitation, immunofluorescence, and immunohistochemistry. Its robustness and versatility make it suitable for use in diverse research areas, such as cancer biology, cell signaling, and drug discovery.

This antibody is produced using state-of-the-art techniques and undergoes stringent quality control measures to ensure batch-to-batch consistency and reproducibility. It is supplied as a purified and concentrated solution, ready for immediate use in experiments.

Choose the NBK(Phospho Thr33) Polyclonal Antibody for its exceptional specificity, sensitivity, and reliability. It is an indispensable tool for researchers seeking to unravel the intricate mechanisms of protein phosphorylation and its impact on cellular processes.