Human ALK-2 / ACVR1 / ALK2 Protein (His Tag)

ACTRI,ACVR1A,ACVRLK2,ALK2,FOP,SKR1,TSRI

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Catalog Number	P10227-H08B
Organism Species	Human
Host	Baculovirus-Insect Cells
Synonyms	ACTRI,ACVR1A,ACVRLK2,ALK2,FOP,SKR1,TSRI
Molecular Weight	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.
predicted N	Met 21
SDS-PAGE
Purity	> 93 % as determined by SDS-PAGE
Protein Construction	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.
Bio-activity	Kinase activity untested
Research Area	Cancer |Invasion microenvironment |Angiogenesis |Growth Factor & Receptor |Transforming Growth Factor Beta (TGF-beta) Superfamily |Transforming Growth Factor Beta (TGF-beta) Family |
Formulation	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.
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).
Reference	Armes NA,et al. (1997) The ALK-2 and ALK-4 activin receptors transduce distinct mesoderm-inducing signals during early Xenopus development but do not co-operate to establish thresholds. Development 124(19): 3797-804. Armes NA, et al. (1999) A short loop on the ALK-2 and ALK-4 activin receptors regulates signaling specificity but cannot account for all their effects on early Xenopus development. J Biol Chem. 274(12):7929-35. Kawai S, et al. (2000) Mouse smad8 phosphorylation downstream of BMP receptors ALK-2, ALK-3, and ALK-6 induces its association with Smad4 and transcriptional activity.Biochem Biophys Res Commun. 271(3):682-7. Deng Y, et al. (2009) Efficient highly selective synthesis of methyl 2-(ethynyl)alk-2(E)-enoates and 2-(1'-chlorovinyl)alk-2(Z)-enoates from 2-(methoxycarbonyl)-2,3-allenols. Organic letters 11(10):2169-72.