|Datasheet||Specific References||Reviews||Related Products||Protocols|
|Vector Type||Mammalian Expression Vector|
|Expression Method||Constiutive, Stable / Transient|
|Selection In Mammalian Cells||Hygromycin|
A polyhistidine-tag is an amino acid motif in proteins that consists of at least five histidine (His) residues, often at the N- or C-terminus of the protein.
Polyhistidine-tags are often used for affinity purification of polyhistidine-tagged recombinant proteins expressed in Escherichia coli and other prokaryotic expression systems.
|Rat ACVR1 ORF mammalian expression plasmid, C-GFPSpark tag||RG80118-ACG|
|Rat ACVR1 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||RG80118-ACR|
|Rat ACVR1 ORF mammalian expression plasmid, C-Flag tag||RG80118-CF|
|Rat ACVR1 ORF mammalian expression plasmid, C-His tag||RG80118-CH|
|Rat ACVR1 ORF mammalian expression plasmid, C-Myc tag||RG80118-CM|
|Rat ACVR1 ORF mammalian expression plasmid, C-HA tag||RG80118-CY|
|Rat ACVR1 Gene cDNA clone plasmid||RG80118-G|
|Rat ACVR1 natural ORF mammalian expression plasmid||RG80118-G-N|
|Rat ACVR1 ORF mammalian expression plasmid, N-Flag tag||RG80118-NF|
|Rat ACVR1 ORF mammalian expression plasmid, N-His tag||RG80118-NH|
|Rat ACVR1 ORF mammalian expression plasmid, N-Myc tag||RG80118-NM|
|Rat ACVR1 ORF mammalian expression plasmid, N-HA tag||RG80118-NY|
|Rat ACVR1 natural ORF mammalian expression plasmid||RG80118-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).