CALR Recombinant Monoclonal Antibody

Uniprot Id

P27797

Target Species

Human

Target Name

CALR

Target Full Name

Calreticulin

Target 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. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis. 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.

Target Subcellular Location

Endoplasmic reticulum lumen. Cytoplasm, cytosol. Secreted, extracellular space, extracellular matrix. Cell surface. Sarcoplasmic reticulum lumen. Cytoplasmic vesicle, secretory vesicle, Cortical granule. Cytolytic granule.

Target Protein Families

Calreticulin family

Target Research Area

Tags & Cell Markers

Target Synonyms

Autoantigen RO; CALR; CALR protein; CALR_HUMAN; Calregulin; Calreticulin; cC1qR; CRP55; CRT; CRTC; Endoplasmic reticulum resident protein 60; Epididymis secretory sperm binding protein Li 99n; ERp60; FLJ26680; grp60; HACBP; HEL S 99n; RO; Sicca syndrome antigen A (autoantigen Ro; calreticulin); Sicca syndrome antigen A; SSA

Target Background

Calreticulin is a highly conserved chaperone protein which resides primarily in the endoplasmic reticulum, and is involved in a variety of cellular processes, among them, cell adhesion. Additionally, it functions in protein folding quality control and calcium homeostasis. Calreticulin is also found in the nucleus, suggesting that it may have a role in transcription regulation. Systemic lupus erythematosus is associated with increased autoantibody titers against calreticulin. Recurrent mutations in calreticulin have been linked to various neoplasms, including the myeloproliferative type.