Mouse ACVR2B (His Tag) recombinant protein

Mouse ACVR2B (His Tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

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.

Activin receptor type-2B

HTX4; ACTR-IIB; MGC116908; MGC118477; ACVR2B; ACTRIIB

P27040

Acvr2b

Human Cells

A DNA sequence encoding the extracellular domain of mouse ACTRIIB (NP_031423.1) (Met 1-Thr 134) was fused with a polyhistidine tag at the C-terminus.

Mouse

The recombinant mouse ACTRIIB/ACVR2B comprises 127 amino acids and has a predicted molecular mass of 14.8 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rmACVR2B is approximately 33-37 kDa due to glycosylation.

> 94 % as determined by SDS-PAGE

1. Measured by its binding ability in a functional ELISA. Immobilized human ACVR2B (Cat:503817) at 10 μg/mL (100 μl/well) can bind biotinylated mouse INHBA-His (Cat:500709), The EC₅₀ of biotinylated mouse INHBA-His (Cat:500709) is 0.161 μg/mL.
2. Measured by its binding ability in a functional ELISA. Immobilized mouse INHBA-his at 10 μg/mL (100 μl/well) can bind human Follistatin Protein, The EC₅₀ of human Follistatin Protein is 0.39 μg/mL.
3. Measured by its ability to neutralize Activin-mediated inhibition on MPC11 cell proliferation. The ED₅₀ for this effect is typically 0.2-0.8 µg/mL in the presence of 10 ng/mL recombinant Activin A.