|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 EFNB1 ORF mammalian expression plasmid, C-GFPSpark tag||HG10894-ACG|
|Human EFNB1 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG10894-ACR|
|Human EFNB1 ORF mammalian expression plasmid, C-Flag tag||HG10894-CF|
|Human EFNB1 ORF mammalian expression plasmid, C-His tag||HG10894-CH|
|Human EFNB1 ORF mammalian expression plasmid, C-Myc tag||HG10894-CM|
|Human EFNB1 ORF mammalian expression plasmid, C-HA tag||HG10894-CY|
|Human EFNB1 Gene cDNA clone plasmid||HG10894-M|
|Human EFNB1 ORF mammalian expression plasmid, N-Flag tag||HG10894-NF|
|Human EFNB1 ORF mammalian expression plasmid, N-His tag||HG10894-NH|
|Human EFNB1 ORF mammalian expression plasmid, N-Myc tag||HG10894-NM|
|Human EFNB1 ORF mammalian expression plasmid, N-HA tag||HG10894-NY|
|Human EFNB1 natural ORF mammalian expression plasmid||HG10894-UT|
|Learn more about expression Vectors|
Ephrin-B1 also known as EFNB1, is a member of the ephrin family. The transmembrane- associated ephrin ligands and their Eph family of receptor tyrosine kinases are expressed by cells of the SVZ. Eph/ephrin interactions are implicated in axon guidance, neural crest cell migration, establishment of segmental boundaries, and formation of angiogenic capillary plexi. Eph receptors and ephrins are divided into two subclasses, A and B, based on binding specificities. Ephrin subclasses are further distinguished by their mode of attachment to the plasma membrane: ephrin-A ligands bind EphA receptors and are anchored to the plasma membrane via a glycosylphosphatidylinositol (GPI) linkage, whereas ephrin-B ligands bind EphB receptors and are anchored via a transmembrane domain. An exception is the EphA4 receptor, which binds both subclasses of ephrins. EphrinB1 and B class Eph receptors provide positional cues required for the normal morphogenesis of skeletal elements. Another malformation, preaxial polydactyly, was exclusively seen in heterozygous females in which expression of the X-linked ephrinB1 gene was mosaic, so that ectopic EphB-ephrinB1 interactions led to restricted cell movements and the bifurcation of digital rays.