|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 Neuropilin-1 ORF mammalian expression plasmid, C-GFPSpark tag||RG80056-ACG|
|Rat Neuropilin-1 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||RG80056-ACR|
|Rat Neuropilin-1 ORF mammalian expression plasmid, C-Flag tag||RG80056-CF|
|Rat Neuropilin-1 ORF mammalian expression plasmid, C-His tag||RG80056-CH|
|Rat Neuropilin-1 ORF mammalian expression plasmid, C-Myc tag||RG80056-CM|
|Rat Neuropilin-1 ORF mammalian expression plasmid, C-HA tag||RG80056-CY|
|Rat Neuropilin-1 Gene cDNA clone plasmid||RG80056-M|
|Rat Neuropilin-1 ORF mammalian expression plasmid, N-Flag tag||RG80056-NF|
|Rat Neuropilin-1 ORF mammalian expression plasmid, N-His tag||RG80056-NH|
|Rat Neuropilin-1 ORF mammalian expression plasmid, N-Myc tag||RG80056-NM|
|Rat Neuropilin-1 ORF mammalian expression plasmid, N-HA tag||RG80056-NY|
|Rat Neuropilin-1 natural ORF mammalian expression plasmid||RG80056-UT|
|Learn more about expression Vectors|
Neuropilin is a type I transmembrane protein and the molecular mass is 120 kDa. Two homologues, Neuropilin-1 and Neuropilin-2, are identified. The primary structure of Neuropilin-1 and Neuropilin-2 is well conserved and is divided into four domains, CUB (a1/a2) domain, FV/FVIII (b1/b2) domain, MAM (c) domain, and (d) domain that contains a transmembrane and a short cytoplasmic region. Neuropilin-1 (NRP1) acts as a receptor for two different extracellular ligands, class 3 semaphorins and specific isoforms of vascular endothelial growth factor. The functions of NRP1 and NRP2 have been extensively studied in neurons where they act in axon guidance and in endothelial cells where they promote angiogenesis and cell migration. Neuropilin-1 is likely to mediate contacts between the dendritic cells and the T lymphocytes via homotypic interactions and is essential for the initiation of the primary immune response. NRP1 is a co-receptor for VEGF receptor-2 (VEGFR2) that enhances the binding of VEGF165 to VEGFR2 and VEGF165-mediated chemotaxis. NRP1 expression is regulated in EC by tumor necrosis factor-alpha, the transcription factors dHAND and Ets-1, and vascular injury. NRP1 upregulation is positively correlated with the progression of various tumors. Overexpression of NRPI in rat tumor cells results in enlarged tumors and substantially enhanced tumor angiogenesis. On the other hand, soluble NRP1 (sNRP1) is an antagonist of tumor angiogenesis.