|Datasheet||Specific References||Reviews||Related Products||Protocols|
|A DNA sequence encoding the extracellular domain (Met 1-Thr 134) of mouse ACVR2B (NP_031423.1) precursor was fused with the Fc region of human IgG1 at the C-terminus.|
|In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.|
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
|> 97 % as determined by SDS-PAGE|
|1. Measured by its ability to bind biotinylated Human INHBA-his (Cat:10429-H08H) in functional ELISA.|
2. Measured by its ability to bind biotinylated mouse INHBA-his (Cat:50659-M08H) in functional ELISA.
3. Measured by its ability to neutralize Activin-mediated inhibition on MPC11 cell proliferation. The ED50 for this effect is typically 10-50 ng/mL in the presence of 10 ng/mL recombinant Activin A.
|< 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 recombinant mouse ACVR2B/Fc is a disulfide-linked homodimer after removal of the signal peptide. The reduced monomer consists of 364 amino acids and has a predicted molecular mass of 41 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rmACVR2B/Fc monomer is approximately 60-65 kDa due to glycosylation.|
|Lyophilized from sterile PBS, pH 7.4|
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.|
ACVR2A and ACVR2B are two activin type II receptors. ACVR2B is integral to the activin and myostatin signaling pathway. Ligands such as activin and myostatin bind to ACVR2A and ACVR2B. Myostatin, a negative regulator of skeletal muscle growth, is regarded as a potential therapeutic target and binds to ACVR2B effectively, and to a lesser extent, to ACVR2A. The structure of human ACVR2B kinase domain in complex with adenine establishes the conserved bilobal architecture consistent with all other catalytic kinase domains. Haplotype structure at the ACVR2B and follistatin loci may contribute to interindividual variation in skeletal muscle mass and strength. Defects in ACVR2B are a cause of left-right axis malformations.