|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.
|Human PVRL1 ORF mammalian expression plasmid, C-GFPSpark tag||HG11611-ACG|
|Human PVRL1 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG11611-ACR|
|Human PVRL1 ORF mammalian expression plasmid, C-Flag tag||HG11611-CF|
|Human PVRL1 ORF mammalian expression plasmid, C-His tag||HG11611-CH|
|Human PVRL1 ORF mammalian expression plasmid, C-Myc tag||HG11611-CM|
|Human PVRL1 ORF mammalian expression plasmid, C-HA tag||HG11611-CY|
|Human PVRL1 Gene cDNA clone plasmid||HG11611-M|
|Human PVRL1 ORF mammalian expression plasmid, N-Flag tag||HG11611-NF|
|Human PVRL1 ORF mammalian expression plasmid, N-His tag||HG11611-NH|
|Human PVRL1 ORF mammalian expression plasmid, N-Myc tag||HG11611-NM|
|Human PVRL1 ORF mammalian expression plasmid, N-HA tag||HG11611-NY|
|Human PVRL1 natural ORF mammalian expression plasmid||HG11611-UT|
|Learn more about expression Vectors|
Poliovirus receptor-related 1 (herpesvirus entry mediator C; nectin-1; CD111), also known as PVRL1 is a cell adhesion molecule belonging to the immunoglobulin superfamily that can bind to virion glycoprotein D (gD) to mediate entry of herpes simplex viruses (HSV) and pseudorabies virus (PRV). CD111/Nectin-1/PVRL1 colocalizes with E-cadherin at adherens junctions in epithelial cells. The disruption of cell junctions can result in the redistribution of nectin-1. To determine whether disruption of junctions by calcium depletion influenced the susceptibility of epithelial cells to viral entry, Madin-Darby canine kidney cells expressing endogenous nectin-1 or transfected human nectin-1 were tested for the ability to bind soluble forms of viral gD and to be infected by HSV and PRV, before and after calcium depletion. It has been revealed that binding of HSV and PRV gD was localized to adherens junctions in cells maintained in normal medium but was distributed, along with nectin-1, over the entire cell surface after calcium depletion. Both the binding of gD and the fraction of cells that could be infected by HSV-1 and PRV were enhanced by calcium depletion. Taken together, CD111/Nectin-1/PVRL1 confined to adherens junctions in epithelial cells is not very accessible to virus, whereas dissociation of cell junctions releases nectin-1 to serve more efficiently as an entry recptor.