|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 C1s ORF mammalian expression plasmid, C-GFPSpark tag||MG50979-ACG|
|Mouse C1s ORF mammalian expression plasmid, C-OFPSpark / RFP tag||MG50979-ACR|
|Mouse C1s ORF mammalian expression plasmid, C-Flag tag||MG50979-CF|
|Mouse C1s ORF mammalian expression plasmid, C-His tag||MG50979-CH|
|Mouse C1s ORF mammalian expression plasmid, C-Myc tag||MG50979-CM|
|Mouse C1s ORF mammalian expression plasmid, C-HA tag||MG50979-CY|
|Mouse C1s Gene cDNA clone plasmid||MG50979-G|
|Mouse C1s ORF mammalian expression plasmid, N-Flag tag||MG50979-NF|
|Mouse C1s ORF mammalian expression plasmid, N-His tag||MG50979-NH|
|Mouse C1s ORF mammalian expression plasmid, N-Myc tag||MG50979-NM|
|Mouse C1s ORF mammalian expression plasmid, N-HA tag||MG50979-NY|
|Mouse C1s natural ORF mammalian expression plasmid||MG50979-UT|
|Learn more about expression Vectors|
Complement is an integral component of the adaptive and innate immune systems and represents one of the major effector systems for the immune responses. The classical complement pathway is triggered by C1, a complex composed of the binding protein C1q and two proenzymes, C1r and C1s. Upon binding of IgG to the head of C1q, C1r undergoes autoactivation and in turn cleaves and activates C1s. C1r and C1s, the proteases responsible for activation and proteolytic activity of the C1 complex of complement, share similar overall structural organizations featuring five nonenzymic protein modules (two CUB modules surrounding a single EGF module, and a pair of CCP modules) followed by a serine protease domain. Besides highly specific proteolytic activities, both proteases exhibit interaction properties associated with their N-terminal regions. In contrast, C1r and C1s widely differ from each other by their glycosylation patterns: both proteins contain Asn-linked carbohydrates, but four glycosylation sites are present on C1r, and only two on C1s. As a highly specific serine protease, C1s executes the catalytic function of the C1 complex: the cleavage of C4 and C2, and thus instigates a sequence of activation steps of other components of the complement system, culminating in the formation of the membrane attack complex which induces cell lysis. Like other complement serine proteases C1s has restricted substrate specificity and it is engaged into specific interactions with other subcomponents of the complement system. The only other protein known to interact with C1s physiologically is SerpinC1, an inhibitor of serine protease, which inhibits C1s activity and thus plays a regulatory role in controlling the function of C1s enzyme.