|Datasheet||Specific References||Reviews||Related Products||Protocols|
|Vector Type||Mammalian Expression Vector|
|Expression Method||Constiutive, Stable / Transient|
|Selection In Mammalian Cells||Hygromycin|
A myc tag can be used in many different assays that require recognition by an antibody. If there is no antibody against the studied protein, adding a myc-tag allows one to follow the protein with an antibody against the Myc epitope. Examples are cellular localization studies by immunofluorescence or detection by Western blotting.
The peptide sequence of the myc-tag is: N-EQKLISEEDL-C (1202 Da). It can be fused to the C-terminus and the N-terminus of a protein. It is advisable not to fuse the tag directly behind the signal peptide of a secretory protein, since it can interfere with translocation into the secretory pathway.
|Mouse CALR ORF mammalian expression plasmid, C-GFPSpark tag||MG51682-ACG|
|Mouse CALR ORF mammalian expression plasmid, C-OFPSpark / RFP tag||MG51682-ACR|
|Mouse CALR ORF mammalian expression plasmid, C-Flag tag||MG51682-CF|
|Mouse CALR ORF mammalian expression plasmid, C-His tag||MG51682-CH|
|Mouse CALR ORF mammalian expression plasmid, C-Myc tag||MG51682-CM|
|Mouse CALR ORF mammalian expression plasmid, C-HA tag||MG51682-CY|
|Mouse CALR Gene cDNA clone plasmid||MG51682-G|
|Mouse CALR ORF mammalian expression plasmid, N-Flag tag||MG51682-NF|
|Mouse CALR ORF mammalian expression plasmid, N-His tag||MG51682-NH|
|Mouse CALR ORF mammalian expression plasmid, N-Myc tag||MG51682-NM|
|Mouse CALR ORF mammalian expression plasmid, N-HA tag||MG51682-NY|
|Mouse CALR natural ORF mammalian expression plasmid||MG51682-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.