CRP;ERp;endoplasmic reticulum resident protein;CaBP;CALR;CRT;HEL-S-99n;RO;SSA;cC1qR;CaBP3;calregulin;Calreticulin;calsequestrin-like protein;CRP55;endoplasmic reticulum resident protein 60;ERp60;CRTC;Autoantigen RO;CALR protein;calreticulin);Epididymis secretory sperm binding protein Li 99n;FLJ26680;grp60;HACBP;HEL S 99n;Sicca syndrome antigen A;Sicca syndrome antigen A (autoantigen Ro

E.coli

Glu18-Leu417

P27797

Human

64.0 kDa

65 kDa

N-Trx

Not validated for activity

> 90% as determined by reducing SDS-PAGE.

< 10 EU/mg of the protein as determined by the LAL method

Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

This product is provided as lyophilized powder which is shipped with ice packs.

Lyophilized from a 0.2 μm filtered solution in PBS with 5% Trehalose and 5% Mannitol.

It is recommended that sterile water be added to the vial to prepare a stock solution of 0.5 mg/mL. Concentration is measured by UV-Vis

Calreticulin is a multifunctional protein. It acts as a main Ca(2+)-binding (storage) protein in the lumen of the endoplasmic reticulum. Calreticulin binds Ca2+ ions (a second messenger in signal transduction), rendering it inactive. The Ca2+ is bound with low affinity, but high capacity, and can be released on a signal. Located in storage compartments associated with the endoplasmic reticulum, calreticulin also binds to misfolded proteins and prevents them from being exported from the endoplasmic reticulum to the golgi apparatus. The amino terminus of calreticulin interacts with the DNA-binding domain of the glucocorticoid receptor and prevents the receptor from binding to its specific glucocorticoid response element. Calreticulin reduces the binding of androgen receptor to its hormone-responsive DNA element and inhibits androgen receptor and retinoic acid receptor transcriptional activities in vivo, as well as retinoic acid-induced neuronal differentiation. Therefore, calreticulin acts as a significant modulator of the regulation of gene transcription by nuclear hormone receptors.