|Datasheet||Specific References||Reviews||Related Products||Protocols|
|Vector Type||Mammalian Expression Vector|
|Expression Method||Constiutive, Stable / Transient|
|Selection In Mammalian Cells||Hygromycin|
A polyhistidine-tag is an amino acid motif in proteins that consists of at least five histidine (His) residues, often at the N- or C-terminus of the protein.
Polyhistidine-tags are often used for affinity purification of polyhistidine-tagged recombinant proteins expressed in Escherichia coli and other prokaryotic expression systems.
|Human CALR ORF mammalian expression plasmid, C-GFPSpark tag||HG13539-ACG|
|Human CALR ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG13539-ACR|
|Human CALR ORF mammalian expression plasmid, C-Flag tag||HG13539-CF|
|Human CALR ORF mammalian expression plasmid, C-His tag||HG13539-CH|
|Human CALR ORF mammalian expression plasmid, C-Myc tag||HG13539-CM|
|Human CALR ORF mammalian expression plasmid, C-HA tag||HG13539-CY|
|Human CALR Gene cDNA clone plasmid||HG13539-G|
|Human CALR ORF mammalian expression plasmid, N-Flag tag||HG13539-NF|
|Human CALR ORF mammalian expression plasmid, N-His tag||HG13539-NH|
|Human CALR ORF mammalian expression plasmid, N-Myc tag||HG13539-NM|
|Human CALR ORF mammalian expression plasmid, N-HA tag||HG13539-NY|
|Human CALR natural ORF mammalian expression plasmid||HG13539-UT|
|Learn more about expression Vectors|
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.