Anti-Human Calreticulin Antibody Pair

Product Description: Calreticulin (CALR) is a multifunctional protein primarily localized in the endoplasmic reticulum (ER), where it serves as a calcium-binding chaperone essential for protein folding and quality control. CALR consists of three distinct domains: an N-terminal domain that facilitates ER localization, a middle proline-rich domain that exhibits lectin-like chaperone activity, and a C-terminal domain containing multiple calcium-binding sites. This protein plays a critical role in maintaining calcium homeostasis within the ER. Beyond its chaperone functions, CALR is also involved in modulating immune responses and cellular metabolism. Its ability to interact with misfolded proteins prevents their export from the ER, thereby ensuring proper protein synthesis and function. Dysregulation of CALR has been linked to several diseases, particularly myeloproliferative neoplasms (MPNs), where somatic mutations in the CALR gene contribute to disease pathogenesis. CALR's role in regulating immune responses has implications in cancer, as it can influence tumor progression and immune evasion. Protein Function: Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (PubMed:7876246). Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (PubMed:11149926). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity). Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and might participate in the block to polyspermy (By similarity) [The Uniprot Consortium]