|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 BPI ORF mammalian expression plasmid, C-GFPSpark tag||HG13907-ACG|
|Human BPI ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG13907-ACR|
|Human BPI ORF mammalian expression plasmid, C-Flag tag||HG13907-CF|
|Human BPI ORF mammalian expression plasmid, C-His tag||HG13907-CH|
|Human BPI ORF mammalian expression plasmid, C-Myc tag||HG13907-CM|
|Human BPI ORF mammalian expression plasmid, C-HA tag||HG13907-CY|
|Human BPI Gene cDNA clone plasmid||HG13907-G|
|Human BPI ORF mammalian expression plasmid, N-Flag tag||HG13907-NF|
|Human BPI ORF mammalian expression plasmid, N-His tag||HG13907-NH|
|Human BPI ORF mammalian expression plasmid, N-Myc tag||HG13907-NM|
|Human BPI ORF mammalian expression plasmid, N-HA tag||HG13907-NY|
|Human BPI natural ORF mammalian expression plasmid||HG13907-UT|
|Learn more about expression Vectors|
Bactericidal/permeability-increasing protein is a member of the BPI/LBP/Plunc superfamily and BPI/LBP family. It is a cationic protein which can be detected in the azurophilic granule and on the surface of polymorphonuclear leukocytes. Bactericidal/permeability-increasing protein also is a lipopolysaccharide binding protein. It is associated with human neutrophil granules and has bactericidal activity on gram-negative organisms. Bactericidal/permeability-increasing protein contains two domains that adopt the same structural fold, even though they have little sequence similarity. It binds to and neutralises lipopolysaccharides from the outer membrane of Gram-negative bacteria. The cytotoxic action of bactericidal/permeability-increasing protein is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope.