Rat ALK-2 / ACVR1 / ALK2 Protein (Fc Tag)
ACVR1, Acvrlk2
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Catalog Number | P80118-R02H |
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Organism Species | Rat |
Host | Human Cells |
Synonyms | ACVR1, Acvrlk2 |
Molecular Weight | The recombinant rat ACVR1/Fc is a disulfide-linked homodimer. The reduced monomer comprises 344 amino acids and has a predicted molecular mass of 38.5 kDa. The apparent molecular mass of the protein is approximately 43 kDa in SDS-PAGE under reducing conditions. |
predicted N | Met 21 |
SDS-PAGE | |
Purity | > 90 % as determined by SDS-PAGE |
Protein Construction | A DNA sequence encoding the rat ACVR1 (P80201) (Met1-Glu123) was expressed, fused with the Fc region of human IgG1 at the C-terminus. |
Bio-activity | |
Research Area | Cancer |Invasion microenvironment |Angiogenesis |Growth Factor & Receptor |Transforming Growth Factor Beta (TGF-beta) Superfamily |Transforming Growth Factor Beta (TGF-beta) Family | |
Formulation | Lyophilized from sterile PBS, pH 7.4 1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA. |
Background | 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). |
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