背景：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）.
仕様
サイズ：1mg
種由来：Human
発現宿主：Baculovirus-Insect Cells
純度：＞93 ％ as determined by reducing SDS-PAGE.
エンドトキシン濃度：＜1.0 EU per μg of the protein as determined by the LAL method.
アクセッションNo.：Q04771
アミノ酸配列：Met 1-Val 124
遺伝子構造：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.
