Recombinant Mouse Activin Receptor 2B/ACVR2B Protein (His Tag)(Active) | PKSM040825

Recombinant Mouse Activin Receptor 2B/ACVR2B Protein (His Tag)(Active) | PKSM040825 | Gentaur US, UK & Europe Disrtribition

Synonyms: 4930516B21Rik;ActRIIB

Active Protein: Active protein

Activity: 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.

Protein Construction: 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.

Fusion Tag: C-His

Species: Mouse

Expressed Host: HEK293 Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 94 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.

Stability and 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.

Molecular Mass: 14.8 kDa

Formulation: Lyophilized from sterile PBS, pH 7.4

Reconstitution: Please refer to the printed manual for detailed information.

Background: 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.

Research Area: N/A