Description
Recombinant Human ALK-2/ACVR1 Protein (Baculovirus, His Tag) | PKSH030419 | Gentaur US, UK & Europe Disrtribition
Synonyms: Activin Receptor Type-1; Activin Receptor Type I; ACTR-I; Activin Receptor-Like Kinase 2; ALK-2; Serine/Threonine-Protein Kinase Receptor R1; SKR1; TGF-B Superfamily Receptor Type I; TSR-I; ACVR1; ACVRLK2;ACVR1A;ACVRLK2;ALK2;FOP;SKR1
Active Protein: N/A
Activity: 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.
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.
Fusion Tag: C-His
Species: Human
Expressed Host: Baculovirus-Insect Cells
Shipping: This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs. Upon receipt, store it immediately at<-20°C.
Purity: > 93 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per µg as determined by the LAL method.
Stability and Storage: Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles.
Molecular Mass: 12.8kDa
Formulation: Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 7.5, 25% glycreol, 5% Trehalose, 5% Mannitol, 0.01 % Tween-80
Reconstitution: Not Applicable
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).
Research Area: Signal Transduction, epigenetics and nuclear signal, Stem cells
