Human Calreticulin (Fc Tag) recombinant protein

Human Calreticulin (Fc Tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

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.

Calreticulin

SSA; ENDOPLASMIC RETICULUM RESIDENT PROTEIN 60; HACBP; CRT; CRP55; CALRETICULIN); SICCA SYNDROME ANTIGEN A (AUTOANTIGEN RO; CALREGULIN; CC1QR; ERP60; GRP60; RO; HEL-S-99N; CALRETICULIN; CALR

P27797

CALR; CRTC

Human Cells

A DNA sequence encoding the human CALR (P27797) (Met1-Ala413) was expressed with the Fc region of human IgG1 at the C-terminus.

Human

The recombinant human CALR/Fc is a disulfide-linked homodimer. The reduced monomer comprises 637 amino acids and has a predicted molecular mass of 73 kDa. The apparent molecular mass of the protein is approximately 96 and 38 kDa in SDS-PAGE under reducing conditions.

(75.9+20.5) % as determined by SDS-PAGE