Anti-Calreticulin [Polyclonal] (56259-100ul)

Calreticulin is a multifunctional highly conserved Ca+2-binding protein that is localized primarily in the endoplasmic reticulum (ER) but has also been detected in the nucleus and nuclear envelope. Like many other ER proteins, it has the conserved ER retention KDEL sequence (Lys-Asp-Glu-Leu) at its C-terminus. Calreticulin is made up of three domains: 1 180 residue N-terminal domain, a proline- rich P-domain (aa 189-288) that binds Ca+2 with high affinity and shares homology with calnexin and calmegin, and a 110 residue C-terminal domain that binds Ca+2 with low affinity but high capacity. Calreticulin appears to be involved in calcium storage and regulation, has molecular chaperone activity, and has been shown to be induced in response to various types of cell stress.