|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 CLPS ORF mammalian expression plasmid, C-GFPSpark tag||HG13631-ACG|
|Human CLPS ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG13631-ACR|
|Human CLPS ORF mammalian expression plasmid, C-Flag tag||HG13631-CF|
|Human CLPS ORF mammalian expression plasmid, C-His tag||HG13631-CH|
|Human CLPS ORF mammalian expression plasmid, C-Myc tag||HG13631-CM|
|Human CLPS ORF mammalian expression plasmid, C-HA tag||HG13631-CY|
|Human CLPS Gene cDNA clone plasmid||HG13631-G|
|Human CLPS ORF mammalian expression plasmid, N-Flag tag||HG13631-NF|
|Human CLPS ORF mammalian expression plasmid, N-His tag||HG13631-NH|
|Human CLPS ORF mammalian expression plasmid, N-Myc tag||HG13631-NM|
|Human CLPS ORF mammalian expression plasmid, N-HA tag||HG13631-NY|
|Human CLPS natural ORF mammalian expression plasmid||HG13631-UT|
|Learn more about expression Vectors|
Colipase belongs to the colipase family. Structural studies of the complex and of colipase alone have revealed the functionality of its architecture. It is a small protein with five conserved disulphide bonds. Structural analogies have been recognised between a developmental protein, the pancreatic lipase C-terminal domain, the N-terminal domains of lipoxygenases and the C-terminal domain of alpha-toxin. Colipase can only be detected in pancreatic acinar cells, suggesting regulation of expression by tissue-specific elements. Colipase allows lipase to anchor noncovalently to the surface of lipid micelles, counteracting the destabilizing influence of intestinal bile salts. Without colipase the enzyme is washed off by bile salts, which have an inhibitory effect on the lipase. Colipase is a cofactor needed by pancreatic lipase for efficient dietary lipid hydrolysis. It binds to the C-terminal, non-catalytic domain of lipase, thereby stabilising as active conformation and considerably increasing the overall hydrophobic binding site.