The gene for calreticulin (CALR) is located on the human chromosome 19p13.13. The encoded protein is a predominantly conserved calcium-binding chaperone, which is localized primarily to the lumen of the endoplasmic reticulum (ER). Calreticulin comprises three domains, a globular N-domain, a proline-rich P-domain, and a highly acidic C-domain.
Anti-Calreticulin recognizes human and dog calreticulin (55-60 kDa).
synthetic peptide corresponding to the C-terminus of human calreticulin (amino acids 401-417).
Anti-Calreticulin antibody produced in rabbit has been used in:
Calreticulin facilitates transient interaction with newly synthesized cellular and extracellular proteins for folding and assembling in the endoplasmic reticulum (ER) before its localization to the cytosol or cell surface. Calreticulin acts as a lectin-like chaperone binding oligosaccharide residues of newly synthesized N-linked glycoproteins and misfolded proteins. It is believed to play a critical role in quality control processes during protein synthesis and folding and calcium (Ca2+) homeostasis. Increased expression of calreticulin increases the 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+-adenosine triphosphatase (ATPase) (SERCA). Overexpression of calreticulin results in increased sensitivity of HeLa cells to drug-induced apoptosis. However, increased resistance to apoptosis has been observed in calreticulin-deficient cells.
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Storage and Stability
Store at -20 °C. For continuous use, the product maybe stored at 2-8 °C for up to one month. For prolonged storage, freeze in working aliquots at-20 °C. Repeated freezing and thawing, or storage in “frost-free” freezers, is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded ifnot used within 12 hours.
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