|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 ENG ORF mammalian expression plasmid, C-GFPSpark tag||RG80140-ACG|
|Rat ENG ORF mammalian expression plasmid, C-OFPSpark / RFP tag||RG80140-ACR|
|Rat ENG ORF mammalian expression plasmid, C-Flag tag||RG80140-CF|
|Rat ENG ORF mammalian expression plasmid, C-His tag||RG80140-CH|
|Rat ENG ORF mammalian expression plasmid, C-Myc tag||RG80140-CM|
|Rat ENG ORF mammalian expression plasmid, C-HA tag||RG80140-CY|
|Rat ENG Gene cDNA clone plasmid||RG80140-G|
|Rat ENG ORF mammalian expression plasmid, N-Flag tag||RG80140-NF|
|Rat ENG ORF mammalian expression plasmid, N-His tag||RG80140-NH|
|Rat ENG ORF mammalian expression plasmid, N-Myc tag||RG80140-NM|
|Rat ENG ORF mammalian expression plasmid, N-HA tag||RG80140-NY|
|Rat ENG natural ORF mammalian expression plasmid||RG80140-UT|
|Learn more about expression Vectors|
Endoglin, also known as CD105, is a type I homodimeric transmembrane glycoprotein with a large, disulfide-linked, extracellular region and a short, constitutively phosphorylated cytoplasmic tail. Endoglin contains an RGD tripeptide which is a key recognition structure in cellular adhesion,,suggesting a critical role for endoglin in the binding of endothelial cells to integrins and/or other RGD receptors. Endoglin is highly expressed on vascular endothelial cells, chondrocytes, and syncytiotrophoblasts of term placenta. It is also found on activated monocytes, mesenchymal stem cells and leukemic cells of lymphoid and myeloid lineages. As an accessory receptor for the TGF-β superfamily ligands, endoglin binds TGF-β1 and TGF-β3 with high affinity not by itself but by associating with TGF-β type I I receptor (TβRII) and activates the downstream signal pathways. In addition, in human umbilical vein endothelial cells, ALK-1 is also a receptor kinase for endoglin threonine phosphorylation, and mutations in either of the two genes result in the autosomal-dominant vascular dysplasia, hereditary hemorrhagic telangiectasia (HHT). Endoglin has been regarded as a powerful biomarker of neovascularization, and is associated with several solid tumor types.