CPM Polyclonal Antibody

Carboxypeptidase M encoded by CPM is a membrane-bound arginine/lysine carboxypeptidase. Its expression is associated with monocyte to macrophage differentiation. This encoded protein contains hydrophobic regions at the amino and carboxy termini and has 6 potential asparagine-linked glycosylation sites. The active site residues of carboxypeptidases A and B are conserved in this protein. Three alternatively spliced transcript variants encoding the same protein have been described for CPM.

The CPM Polyclonal Antibody is a highly specific and reliable tool designed for the detection and quantification of Carboxypeptidase M (CPM) protein in various biological samples. This antibody is produced through a rigorous process, ensuring its exceptional quality and performance.

With its polyclonal nature, this antibody exhibits a broad reactivity, allowing for the detection of CPM protein across multiple species. It has been extensively validated in various experimental settings, including Western blotting, immunohistochemistry, and immunofluorescence, guaranteeing its versatility and accuracy.

The CPM Polyclonal Antibody offers exceptional sensitivity, enabling the detection of low-abundance CPM protein with utmost precision. Its high affinity ensures minimal background noise, resulting in clear and reliable results. This antibody is an indispensable tool for researchers and scientists working in the fields of biochemistry, molecular biology, and cell biology.

Furthermore, the CPM Polyclonal Antibody is supplied in a convenient and user-friendly format, allowing for easy handling and storage. It is provided in a liquid form, eliminating the need for reconstitution, and is stable for long-term storage at recommended temperatures.

In summary, the CPM Polyclonal Antibody is a superior product that guarantees accurate and reliable detection of Carboxypeptidase M protein. Its exceptional sensitivity, broad reactivity, and user-friendly format make it an essential tool for various research applications.