Anti-CALR Antibody

Calreticulin, encoded by the CALR gene, is a calcium-binding chaperone resident in the lumen of the endoplasmic reticulum. It guides nascent glycoprotein folding, contributes to quality control of newly synthesized proteins, and buffers intracellular calcium stores. Beyond its housekeeping role inside the ER, cell-surface calreticulin acts as an immunogenic "eat-me" signal during immunogenic cell death, promoting phagocytic clearance and supporting dendritic cell-mediated antitumor immunity. The protein also participates in antigen processing, thrombospondin-1 signaling, cardiac and embryonic development, wound healing, and adipogenic differentiation.

This unconjugated rabbit polyclonal reagent from Antibodies.com is validated for western blot, immunohistochemistry, and immunofluorescence workflows on human, mouse, and rat samples, supplied as 100 µl of liquid antiserum for use as a primary antibody in standard immunodetection protocols. It is relevant to research on endoplasmic reticulum stress and the unfolded protein response, the diagnostic CALR exon 9 mutations found in essential thrombocythemia and primary myelofibrosis, integrin-dependent cell adhesion, MHC class I peptide loading, and investigations of glioblastoma and other solid tumor biology. Storage at -20 °C in working aliquots helps preserve reactivity across repeated freeze-thaw cycles.