Related Products

Molecular

Species

Protein

Antibody

Application

cDNA ORF Clone 
Cell Lysate 
qPCR 

ALK2

Human

10227-H03H
C-human IgG1-Fc&His&Active

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10227-H08B
C-His

10227-T24
Rabbit IgG PAb,Antigen Affinity Purified

ELISA,IHC-P

Rat

80118-R02H
C-human IgG1-Fc

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Mouse

50297-M03H
C-human IgG1-Fc&His&Active

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Canine

70048-D08H
C-His

70048-T48
Rabbit IgG PAb,Antigen Affinity Purified

ELISA,WB

70048-D02H
C-human IgG1-Fc

/

/

Cynomolgus

90058-C02H
C-human IgG1-Fc

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   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).