Overview
Rat calreticulin (CALR) is a multifunctional endoplasmic reticulum (ER)-resident protein with critical roles in calcium signaling and protein quality control. As a member of the calnexin/calreticulin family, it assists in glycoprotein folding via the ER's chaperone system. The protein also translocates to the cell surface under stress conditions, where it mediates immunogenic cell death and phagocytosis signaling. In research settings, rat calreticulin serves as a model for studying conserved molecular mechanisms across mammals. Its sequence shares ~90% homology with human CALR, making it particularly valuable for translational studies in autoimmune disorders (e.g., rheumatoid arthritis) and cancer immunotherapy development.
Physical and Chemical Properties
Rat calreticulin is a globular protein with three domains: N-terminal, proline-rich P-domain, and C-terminal calcium-binding region. The P-domain contains conserved motifs that interact with ERp57 for disulfide bond formation during glycoprotein folding. The C-terminal domain binds up to 25 Ca²⁺ ions with low affinity (Kd ~2mM), functioning as a dynamic calcium buffer. The protein exhibits pH-dependent solubility, remaining stable between pH 6.0-8.0. Its secondary structure comprises ~40% β-sheets and ~10% α-helices, as confirmed by circular dichroism spectroscopy. Under non-reducing conditions, it migrates at ~48kDa on SDS-PAGE due to post-translational modifications, though the calculated mass from its 417-amino acid sequence is approximately 46kDa.
Main Applications
In biomedical research, rat calreticulin is primarily used to investigate ER stress responses and unfolded protein response (UPR) pathways. Researchers employ knockout models to study its role in cardiac development, where CALR deficiency leads to impaired calcium handling and embryonic lethality. The protein also has emerging applications in oncology. Surface-exposed calreticulin serves as an 'eat-me' signal for dendritic cells, making it a target for enhancing immunogenic cell death during chemotherapy. Recent studies utilize recombinant rat CALR to standardize assays measuring immunogenic potential in preclinical cancer models.
Safety and Storage
While rat calreticulin itself isn't classified as hazardous, proper handling procedures should be followed to prevent contamination. Use gloves and work in a laminar flow hood when reconstituting lyophilized protein. Avoid vortexing to prevent aggregation—gentle pipetting is recommended for solution preparation. For long-term storage, aliquot the protein in working concentrations (typically 0.1-1mg/mL) with carrier proteins like BSA (0.1%) to prevent surface adsorption. Lyophilized powder remains stable for ≥2 years at -20°C, while solutions retain activity for 3-6 months when stored at -80°C with minimal freeze-thaw cycles.
B2B Procurement Guide
When sourcing rat calreticulin for research, prioritize suppliers that provide batch-specific certificates of analysis (CoA) detailing purity (≥90% by HPLC), endotoxin levels, and functional validation data. Common validation methods include calcium-binding assays (e.g., Quin-2 fluorescence) and chaperone activity tests using denatured substrates. For immunological studies, opt for low-endotoxin variants (<0.1EU/μg). Bulk purchasers (≥10mg) should negotiate pricing tiers and request stability data under shipping conditions. Leading suppliers include Sigma-Aldrich (Product #C7617), Abcam (ab2907), and R&D Systems (custom recombinant production services).
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