|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 EphB6 ORF mammalian expression plasmid, C-GFPSpark tag||HG10197-ACG|
|Human EphB6 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG10197-ACR|
|Human EphB6 ORF mammalian expression plasmid, C-Flag tag||HG10197-CF|
|Human EphB6 ORF mammalian expression plasmid, C-His tag||HG10197-CH|
|Human EphB6 ORF mammalian expression plasmid, C-Myc tag||HG10197-CM|
|Human EphB6 ORF mammalian expression plasmid, C-HA tag||HG10197-CY|
|Human EphB6 Gene cDNA clone plasmid||HG10197-M|
|Human EphB6 ORF mammalian expression plasmid, N-Flag tag||HG10197-NF|
|Human EphB6 ORF mammalian expression plasmid, N-His tag||HG10197-NH|
|Human EphB6 ORF mammalian expression plasmid, N-Myc tag||HG10197-NM|
|Human EphB6 ORF mammalian expression plasmid, N-HA tag||HG10197-NY|
|Human EphB6 natural ORF mammalian expression plasmid||HG10197-UT|
|Learn more about expression Vectors|
Ephrins are divided into the ephrin-A (EFNA) class and the ephrin-B (EFNB) class based on their structures and sequence relationships. Ephrin receptors make up the largest subgroup of the receptor tyrosine kinase (RTK) family. EphB6 is an unusual Eph receptor, lacking catalytic capacity due to alterations in its kinase domain. Interestingly, increased metastatic activity is associated with reduced EphB6 receptor expression in several tumor types, including breast cancer. This emphasizes the potential of EphB6 to act as a suppressor of cancer aggressiveness. EphB6 suppress cancer invasiveness through c-Cbl-dependent signaling, morphologic changes, and cell attachment and indicate that EphB6 may represent a useful prognostic marker and a promising target for therapeutic approaches. EphB6 can both positively and negatively regulate cell adhesion and migration, and suggest that tyrosine phosphorylation of the receptor by an Src family kinase acts as the molecular switch for the functional transition. In addition, Ephrin-B2 may be a physiological ligand for the EphB6 receptor.