|Datasheet||Specific References||Reviews||Related Products||Protocols|
|ACVR1, ACTRI, ACVR1A, ACVRLK2, ALK2, FOP, SKR1, TSRI|
|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.|
|Kinases are highly recommended to be shipped at frozen temperature with blue ice or dry ice.|
Shipment made at ambient temperature may seriously affect the activity of the ordered products.
|> 93 % as determined by SDS-PAGE|
|Kinase activity untested|
|< 1.0 EU per μg of the protein as determined by the LAL method|
|Samples are stable for up to twelve months from date of receipt at -70℃|
|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.|
|Supplied as sterile 20mM Tris, 500mM NaCl, pH 7.4, 10% gly|
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
|Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.|
|A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.|
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).