Monoclonal Anti-Calreticulin (mouse IgG1 isotype) is derived from the hybridoma TO-11 produced by the fusion of mouse myeloma cells (P3-X63-AG8.653 cells) and splenocytes from BALB/c mice. Calreticulin is a molecular chaperones in endoplasmic reticulum lumen. Calreticulin acts as a lectin-like chaperone binding oligosaccharide residues of newly synthesized N-linked glycoproteins, and misfolded proteins. Calreticulin is a protein binding Ca²⁺ ions. It is encoded by the CALR gene in humans.

Monoclonal Anti-Calreticulin antibody produced in mouse is suitable for the following applications:

• Flow cytometry
• Immunocytochemistry
• Immunohistochemistry
• Indirect ELISA
• Western blotting

Calreticulin and Its variants causes differential effects on thrombopoiesis. Somatic mutations of calreticulin (CALR) gene causes thrombocythemia (ET) and primary myelofibrosis (PMF).

It is believed to play a critical role in quality control processes during protein synthesis and folding. Increased expression of calreticulin increases Ca²⁺ storage capacity of the ER. It also appears to modulate store-operated Ca²⁺ -influx, and to alter Ca²⁺ transport by the sarcoplasmic/ER Ca²⁺ -ATPase (SERCA). Overexpression of calreticulin results in increased sensitivity of HeLa cells to drug-induced apoptosis. In contrast, calreticulin-deficient cells show increased resistance to apoptosis. Calreticulin gene disruption leads toimpairment of cardiac development. Loss of calreticulin function favors ubiquitin-proteosome activity. It plays a critical role in Ca²⁺ homeostasis.

Culture supernatant solution containing 15 mM sodium azide.

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