Human ALK-2 / ACVR1 (His Tag) recombinant protein
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).
Activin receptor type-1
Protein short names
ACVRLK2; ALK-2; FOP; SKR1; ACTRI; TSRI; ACVR1; D330013D15RIK; TSK7L; ACTRIA; RP23-100B18.4; ACTR-I; ACVR; ALK2; ACVR1A; ALK8
A DNA sequence encoding the extracellular domain (Met 1-Val 124) of human ALK2 (Q04771) (Met 1-Val 124) was fused with a polyhistidine tag at the C-terminus.
The secreted recombinant human ALK2 consists of 114 amino acids and has a calculated molecular mass of 12.8KDa. It migrates as an approximately 17 kDa band in SDS-PAGE under reducing conditions.
> 93 % as determined by SDS-PAGE
Kinase activity untested
Human ALK-2 / ACVR1 / ALK2 Protein (His Tag) SDS-PAGE
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