Calnexin Polyclonal Antibody

CANX encodes a member of the calnexin family of molecular chaperones. Calnexin is a calcium-binding, endoplasmic reticulum (ER)-associated protein that interacts transiently with newly synthesized N-linked glycoproteins, facilitating protein folding and assembly. It may also play a central role in the quality control of protein folding by retaining incorrectly folded protein subunits within the ER for degradation. Alternatively spliced transcript variants encoding the same protein have been described

The Calnexin Polyclonal Antibody is a highly specific and reliable tool designed for the detection and analysis of calnexin protein in various biological samples. This antibody is produced using advanced immunization techniques, ensuring high affinity and sensitivity towards the target protein.

Calnexin is an integral membrane protein primarily localized in the endoplasmic reticulum (ER) and plays a crucial role in protein folding and quality control. It interacts with newly synthesized glycoproteins, facilitating their proper folding and preventing their premature degradation. The Calnexin Polyclonal Antibody recognizes the conserved regions of calnexin, enabling accurate detection and quantification of this protein in a wide range of species.

This antibody has been extensively validated for various applications, including Western blotting, immunohistochemistry, and immunofluorescence. It exhibits minimal cross-reactivity with other related proteins, ensuring specific and reliable results. The Calnexin Polyclonal Antibody demonstrates excellent performance in both research and diagnostic settings, making it an ideal choice for scientists and clinicians alike.

With its high quality and consistent performance, the Calnexin Polyclonal Antibody is an indispensable tool for studying the intricate mechanisms of protein folding and ER quality control. Its versatility and reliability make it an essential component of any laboratory or research facility focused on understanding cellular processes and disease mechanisms.