MYH-pan (Acetyl Lys1394) Rabbit Polyclonal Antibody

Myosin is a major contractile protein which converts chemical energy into mechanical energy through the hydrolysis of ATP. Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. Myosin heavy chains are encoded by a multigene family. In mammals at least 10 different myosin heavy chain (MYH) isoforms have been described from striated| smooth| and nonmuscle cells. These isoforms show expression that is spatially and temporally regulated during development.

The MYH-pan (Acetyl Lys1394) Rabbit Polyclonal Antibody is a highly specific and sensitive immunological reagent designed for the detection and quantification of MYH-pan protein in various biological samples. This antibody is produced by immunizing rabbits with a synthetic peptide corresponding to the acetylated lysine 1394 of the MYH-pan protein. The resulting polyclonal antibody exhibits high affinity and specificity towards the acetylated form of MYH-pan, making it an ideal tool for studying the post-translational modifications of this protein.

The MYH-pan (Acetyl Lys1394) Rabbit Polyclonal Antibody has been extensively validated for use in various applications, including Western blotting, immunoprecipitation, and immunohistochemistry. It has been shown to detect endogenous levels of acetylated MYH-pan in various cell lines and tissues, and can be used to monitor changes in MYH-pan acetylation levels under different experimental conditions.

This antibody is supplied as a purified IgG fraction, and has been affinity-purified using a peptide column to ensure maximum specificity and minimal cross-reactivity. It is provided in a convenient 100 µg size, and is suitable for use in both research and diagnostic applications.

Overall, the MYH-pan (Acetyl Lys1394) Rabbit Polyclonal Antibody is a reliable and high-quality reagent that can be used to study the role of MYH-pan in various biological processes, and to investigate the mechanisms underlying its post-translational modifications.