|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||48142 Da|
|Application & Usage||Western blot analysis (0.5-4 µg/ml) and in Immunohistochemistry (10-20 µg/ml). However, the optimal conditions should be determined individually.|
|Other Names||CRP55, CRTC, CALR, Calregulin, cC1qR, ERp60, HACBP, RO, SSA,|
|Formulation||100 µg (200 µg/ml) protein A purified antibody in PBS containing 30% glycerol, 0.5 mg/ml BSA, and 0.01% thimerosal.|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||Calreticulin Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|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 (By similarity).|
|Cellular Location||Endoplasmic reticulum lumen. Cytoplasm, cytosol. Secreted, extracellular space, extracellular matrix. Cell surface. Sarcoplasmic reticulum lumen. Note=Also found in cell surface (T cells), cytosol and extracellular matrix Associated with the lytic granules in the cytolytic T-lymphocytes|
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Provided below are standard protocols that you may find useful for product applications.
Calreticulin is a calcium binding protein found in abundance in the endoplasmic reticulum and the sarcoplasmic reticulum. Like many other ER proteins, it has the conserved ER retention KDEL (Lys-Asp-Glu-Leu) sequence at its C-terminus. Calreticulin has also been detected in the nucleus and nuclear envelop. Recent studies s µggest that this soluble ER protein has a multifunctional role as it appears to be involved in calcium storage and regulation as well as having a molecular chaperone activity. Studies also s µggest its involvement in certain autoimmune diseases. Consistence with its multiple functions the calreticulin molecule appears to have a zonal character. The protein has both high and low affinity calcium binding sites.
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