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Recombinant Human ALK-2/ACVR1 Protein (Baculovirus, His Tag)
SKU: PKSH030419-100
Recombinant Human ALK-2/ACVR1 Protein (Baculovirus, His Tag)
| SKU # | PKSH030419 |
| Expression Host | Baculovirus-Insect Cells |
Description
| Synonyms | ACTR-I, ACVR1, ACVR1A, ACVRLK2, ALK-2, ALK2, Activin Receptor Type I, Activin Receptor Type-1, Activin Receptor-Like Kinase 2, FOP, SKR1, Serine/Threonine-Protein Kinase Receptor R1, TGF-B Superfamily Receptor Type I, TSR-I |
| Species | Human |
| Expression Host | Baculovirus-Insect Cells |
| Sequence | Met 1-Val 124 |
| Accession | Q04771 |
| Calculated Molecular Weight | 12.8 kDa |
| Observed Molecular Weight | 17 kDa |
| Tag | C-His |
| Bio-activity | Not validated for activity |
Properties
| Purity | > 93 % as determined by reducing SDS-PAGE. |
| Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
| Storage | Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles. |
| 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. |
| Formulation | Supplied as sterile solution of 20mM Tris, 500mM NaCl, pH 7.4, 10% glycerol |
| 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).