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Recombinant Mouse ALK-2/ACVR1 Protein (His & Fc Tag)

Cat:PKSM040751
Manual MSDS

Price: $ 1210

Size:
200μg
Quantity:
  • Expression Host: HEK293 Cells
  • Accession: NP_031420.2
  • Applications: ELISA
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Product Details
Synonyms ActR-I;ActRIA;Acvr;Acvrlk2;Alk-2;ALK2;Alk8;D330013D15Rik;SKR1;Tsk7L
Species Mouse
Expression Host HEK293 Cells
Sequence Met 1-Glu 123
Accession NP_031420.2
Calculated Molecular Weight 40 kDa
Observed Molecular Weight 45 kDa
Tag C-His-Fc
Bio-activity Measure by its ability to bind with human BMP2 in a functional ELISA.
Purity > 90 % as determined by reducing SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method.
Storage Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Shipping This product is provided as lyophilized powder which is shipped with ice packs.
Formulation Lyophilized from sterile PBS, pH 7.4
Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.
Reconstitution Please refer to the printed manual for detailed information.
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).