|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.
|Mouse CD95 / Fas ORF mammalian expression plasmid, C-GFPSpark tag||MG50027-ACG|
|Mouse CD95 / Fas ORF mammalian expression plasmid, C-OFPSpark / RFP tag||MG50027-ACR|
|Mouse CD95 / Fas ORF mammalian expression plasmid, C-Flag tag||MG50027-CF|
|Mouse CD95 / Fas ORF mammalian expression plasmid, C-His tag||MG50027-CH|
|Mouse CD95 / Fas ORF mammalian expression plasmid, C-Myc tag||MG50027-CM|
|Mouse CD95 / Fas ORF mammalian expression plasmid, C-HA tag||MG50027-CY|
|Mouse CD95 / Fas ORF mammalian expression plasmid, N-Flag tag||MG50027-NF|
|Mouse CD95 / Fas ORF mammalian expression plasmid, N-His tag||MG50027-NH|
|Mouse CD95 / Fas ORF mammalian expression plasmid, N-Myc tag||MG50027-NM|
|Mouse CD95 / Fas ORF mammalian expression plasmid, N-HA tag||MG50027-NY|
|Mouse CD95 / Fas Gene cDNA clone plasmid||MG50027-U|
|Mouse CD95 / Fas natural ORF mammalian expression plasmid||MG50027-UT|
|Learn more about expression Vectors|
CD95 (APO-1/Fas) is an important inducer of the extrinsic apoptosis signaling pathway and therapy induced apoptosis of many tumor cells has been linked to the activity of CD95. is a prototype death receptor characterized by the presence of an 80 amino acid death domain in its cytoplasmic tail. This domain is essential for the recruitment of a number of signaling components upon activation by either agonistic anti-CD95 antibodies or cognate CD95 ligand that initiate apoptosis. The complex of proteins that forms upon triggering of CD95 is called the death-inducting signaling complex (DISC). The DISC consists of an adaptor protein and initiator caspases and is essential for induction of apoptosis. CD95 is also crucial for the negative selection of B cells within the germinal center (GC). Impairment of CD95-mediated apoptosis results in defective affinity maturation and the persistence of autoreactive B-cell clones. Changes in the expression of CD95 and/or its ligand CD95L are frequently found in human cancer. The downregulation or mutation of CD95 has been proposed as a mechanism by which cancer cells avoid destruction by the immune system through reduced apoptosis sensitivity. Thus, CD95 has therefore been viewed as a tumor suppressor. CD95 has been reported to be involved in the activation of NF-kappaB, MAPK3/ERK1, MAPK8/JNK, and the alternate pathways for CTL-mediated cytotoxicity. Accordingly, this protein is implicated in the pathogenesis of various malignancies and diseases of the immune system. The CD95/CD95L system was implicated in the etiology of inflammatory bowel disease (IBD) based, primarily, on the finding that CD95 is highly expressed in the intestinal epithelial cells and that epithelial apoptosis is increased in IBD.