Calreticulin, also called CALR, is an endoplasmic reticulum (ER) protein that functions as a calcium (Ca2+) buffering molecular chaperone. Together with calnexin and ERp57, calreticulin has a critical role in protein folding and quality control of newly synthesized glycoproteins. Calreticulin has many diverse functions beyond Ca2+ binding, including cell adhesion, lectin binding, apoptosis, nuclear transport, antigen presentation, and immune response. Specifically, calreticulin is part of the peptide-loading complex that resides on the ER membrane and is responsible for antigen loading onto MHC class I molecules.
Calreticulin protein has a theoretical molecular weight of 46 kDa and is 417 amino acids (aa) in length. The protein has three main domains: the N-terminal lectin-like domain, the proline-rich P-domain, and the acidic C-domain which is followed by an ER-retention KDEL signal sequence.
Given its role in multiple biological processes, it makes sense that calreticulin is implicated in both healthy and disease states. Studies have found that calreticulin mutations were present in patients with myeloproliferative neoplasms (MFN) and essential thrombocythaemia (ET). Calreticulin expression is typically upregulated in most cancer lines, however it is downregulated in some tissues including cervical carcinomas, prostate cancer, and human colon adenocarcinoma. High expression of calreticulin on cancer cells is related to tumor cell phagocytosis and is often correlated with, and counteracted by, elevated CD47 expression to prevent cancer cell phagocytosis. Calreticulin mutations can serve as a major diagnostic biomarker for MFN and ET and additionally the calreticulin gene may be a potential target for cancer therapeutics.
Type: Primary
Antigen:
Clonality: Monoclonal
Clone: 1G6A7
Conjugation: Allophycocyanin
Epitope:
Host: Mouse
Isotype: IgG2a
Reactivity: Human, Mouse
