|Datasheet||Specific References||Reviews||Related Products||Protocols|
|Vector Type||Mammalian Expression Vector|
|Expression Method||Constiutive, Stable / Transient|
|Selection In Mammalian Cells||Hygromycin|
Human influenza hemagglutinin (HA) is a surface glycoprotein required for the infectivity of the human virus. The HA tag is derived from the HA-molecule corresponding to amino acids 98-106 has been extensively used as a general epitope tag in expression vectors. Many recombinant proteins have been engineered to express the HA tag, which does not appear to interfere with the bioactivity or the biodistribution of the recombinant protein. This tag facilitates the detection, isolation, and purification of the proteins.
The actual HA tag is as follows: 5' TAC CCA TAC GAT GTT CCA GAT TAC GCT 3' or 5' TAT CCA TAT GAT GTT CCA GAT TAT GCT 3' The amino acid sequence is: YPYDVPDYA.
|Rat CALR ORF mammalian expression plasmid, C-GFPSpark tag||RG81126-ACG|
|Rat CALR ORF mammalian expression plasmid, C-OFPSpark / RFP tag||RG81126-ACR|
|Rat CALR ORF mammalian expression plasmid, C-Flag tag||RG81126-CF|
|Rat CALR ORF mammalian expression plasmid, C-His tag||RG81126-CH|
|Rat CALR ORF mammalian expression plasmid, C-Myc tag||RG81126-CM|
|Rat CALR ORF mammalian expression plasmid, C-HA tag||RG81126-CY|
|Rat CALR ORF mammalian expression plasmid, N-Flag tag||RG81126-NF|
|Rat CALR ORF mammalian expression plasmid, N-His tag||RG81126-NH|
|Rat CALR ORF mammalian expression plasmid, N-Myc tag||RG81126-NM|
|Rat CALR ORF mammalian expression plasmid, N-HA tag||RG81126-NY|
|Rat CALR Gene cDNA clone plasmid||RG81126-U|
|Rat CALR natural ORF mammalian expression plasmid||RG81126-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.