|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 ACVR1 ORF mammalian expression plasmid, C-GFPSpark tag||HG14875-ACG|
|Human ACVR1 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG14875-ACR|
|Human ACVR1 ORF mammalian expression plasmid, C-Flag tag||HG14875-CF|
|Human ACVR1 ORF mammalian expression plasmid, C-His tag||HG14875-CH|
|Human ACVR1 ORF mammalian expression plasmid, C-Myc tag||HG14875-CM|
|Human ACVR1 ORF mammalian expression plasmid, C-HA tag||HG14875-CY|
|Human ACVR1 Gene cDNA clone plasmid||HG14875-G|
|Human ACVR1 ORF mammalian expression plasmid, N-Flag tag||HG14875-NF|
|Human ACVR1 ORF mammalian expression plasmid, N-His tag||HG14875-NH|
|Human ACVR1 ORF mammalian expression plasmid, N-Myc tag||HG14875-NM|
|Human ACVR1 ORF mammalian expression plasmid, N-HA tag||HG14875-NY|
|Human ACVR1 natural ORF mammalian expression plasmid||HG14875-UT|
|Learn more about expression Vectors|
ALK-2, also termed as ACVR1, was initially identified as an activin type I receptor because of its ability to bind activin in concert with ActRII or ActRIIB. ALK-2 is also identified as a BMP type I receptor. It has been demonstrated that ALK-2 forms complex with either the BMP-2/7-bound BMPR-II or ACVR2A /ACVR2B. ALK-1 and ALK-2 presenting in the yeast Saccharomyces cerevisiae are two haspin homologues. Both ALK-1 and ALK-2 exhibit a weak auto-kinase activity in vitro, and are phosphoproteins in vivo. ALK-1 and ALK-2 levels peak in mitosis and late-S/G2. Control of protein stability plays a major role in ALK-2 regulation. The half-life of ALK-2 is particularly short in G1. Overexpression of ALK-2, but not of ALK-1, causes a mitotic arrest, which is correlated to the kinase activity of the protein. This suggests a role for ALK-2 in the control of mitosis. Endoglin is phosphorylated on cytosolic domain threonine residues by the TGF-beta type I receptors ALK-2 and ALK-5 in prostate cancer cells. Endoglin did not inhibit cell migration in the presence of constitutively active ALK-2. Defects in ALK-2 are a cause of fibrodysplasia ossificans progressiva (FOP).