|Datasheet||Specific References||Reviews||Related Products||Protocols|
The pGEM-T is 3kb in length, and contains the amplicin resistance gene, conferring selection of the plasmid in E. coli, and the ori site which is the bacterial origin of replication. The plasmid has multiple cloning sites as shown below. The coding sequence was inserted by TA cloning. Many E. coli strains are suitable for the propagation of this vector including JM109, DH5α and TOP10.
The coding sequence can be easily obtained by digesting the vector with proper restriction enzyme(s). The coding sequence can also be amplified by PCR with M13 primers, or primer pair SP6 and T7.
|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 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.