Recombinant Mouse ACVR2B Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0079

Recombinant Mouse ACVR2B Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0079
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

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Product Overview

Tag His
Host Species Mouse
Accession NP_031423.1
Synonym 4930516B21Rik, ActRIIB
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.
Description A DNA sequence encoding the extracellular domain of mouse ACTRIIB (NP_031423.1) (Met 1-Thr 134) was fused with a His tag at the C-terminus.
Source HEK293
Predicted N Terminal Ser l9
AA Sequence Met 1-Thr 134
Molecular Weight The recombinant mouse ACTRIIB/ACVR2B comprises 127 a.a. 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.
Purity >94% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity 1. Measured by its binding ability in a functional ELISA. Immobilized human ACVR2B at 10 ug/mL (100 ul/well) can bind biotinylated mouse INHBA-His, The EC50 of biotinylated mouse INHBA-His is 0.161 ug/mL.2. Measured by its binding ability in a functional ELISA. Immobilized mouse INHBA-his at 10 ug/mL (100 ul/well) can bind- human Follistatin Protein, The EC50 of human Follistatin Protein is 0.39 ug/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.
Formulation Lyophilized from sterile PBS, pH 7.4.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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