|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.
|Rhesus LAYN ORF mammalian expression plasmid, C-GFPSpark tag||CG90160-ACG|
|Rhesus LAYN ORF mammalian expression plasmid, C-OFPSpark / RFP tag||CG90160-ACR|
|Rhesus LAYN ORF mammalian expression plasmid, C-Flag tag||CG90160-CF|
|Rhesus LAYN ORF mammalian expression plasmid, C-His tag||CG90160-CH|
|Rhesus LAYN ORF mammalian expression plasmid, C-Myc tag||CG90160-CM|
|Rhesus LAYN ORF mammalian expression plasmid, C-HA tag||CG90160-CY|
|Rhesus LAYN Gene cDNA clone plasmid||CG90160-G|
|Rhesus LAYN ORF mammalian expression plasmid, N-Flag tag||CG90160-NF|
|Rhesus LAYN ORF mammalian expression plasmid, N-His tag||CG90160-NH|
|Rhesus LAYN ORF mammalian expression plasmid, N-Myc tag||CG90160-NM|
|Rhesus LAYN ORF mammalian expression plasmid, N-HA tag||CG90160-NY|
|Rhesus LAYN natural ORF mammalian expression plasmid||CG90160-UT|
|Learn more about expression Vectors|
Layilin, a recently characterized as a 55 kDa transmembrane protein with homology to C-type lectins, is present in numerous cell lines and tissue extracts. As one of the adaptor proteins, talin mediates the interactions between the actin filaments and the cell membrane by binding to integral membrane proteins and to the cytoskeleton. Layilin is a newly identified membrane-binding site for talin in peripheral ruffles of spreading cells, a ten-amino acid motif in the layilin cytoplasmic domain is sufficient for talin binding, and its adjacent LH2-LH3 tandem arrays in the cytoplasmic domain provide docking sites for talin. Furthermore, talin binds layilin, PIPK1gamma and integrins in similar although subtly different ways. Layilin binds specifically to hyaluronan (HA) through its extracellular domain, a ubiquitous extracellular matrix component in most animal tissues and body fluids, but not to other tested glycosaminoglycans. The research suggests that layilin may mediate signals from extracellular matrix to the cell cytoskeleton via interaction with different intracellular binding partners and thereby be involved in the modulation of cortical structures in the cell. All the above actions reveal an interesting parallel between layilin and the known HA receptor CD44. In addition, merlin and radixin have been identified as different intracellular binding partners of layilin. Accordingly, it has been suggested that layilin plays roles in a variety of cellular processes, including cell shape, adhesion, motility, and homeostasis, as well as signal transduction. In addition, layilin might play an important role in the process of invasion and lymphatic metastasis of lung carcinoma.