Recombinant human CALR protein with C-terminal human Fc tag
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Amount : | 50 µg |
Purification : | The purity of the protein is greater than 95% as determined by SDS-PAGE and Coomassie blue staining. |
Content : | Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose is added as protectants before lyophilization. |
Storage condition : | Store at -80°C for 12 months (Avoid repeated freezing and thawing) |
Alternative Name : | cC1qR, CRT, HEL-S-99n, RO, SSA |
Expression Host : HEK293
The protein has a predicted molecular mass of 79.53 kDa after removal of the signal peptide.
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.
The protein has a predicted molecular mass of 79.53 kDa after removal of the signal peptide.
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.
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