Recombinant Human ACVR2B Protein (Fc Tag)

Name: Recombinant Human ACVR2B Protein (Fc Tag)
Brand: Beta LifeScience
SKU: BLPSN-0076
Availability: InStock

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, Recombinant proteins

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Product Overview

Tag	Fc
Host Species	Human
Accession	NP_001097.2
Synonym	Activin RIIB, ActR-IIB, ACTRIIB, HTX4
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 N-terminal segment (Met 1-Thr 134) from the extracellular domain of human ACVR2B (NP_001097.2) was expressed with the fused human IgG1 Fc region at the C-terminus.
Source	HEK293
Predicted N Terminal	Ser 19
AA Sequence	Met 1-Thr 134
Molecular Weight	The recombinant human ACVR2B/Fc chimera is a disulfide-linked homodimer generated after removal of the signal peptide. The reduced monomer comprises 354 a.a. and predicts a molecular mass of 40.0 kDa. As a result of glycosylation, the monomer migrates as an approximately 60-65 kDa protein in SDS-PAGE under reducing conditions.
Purity	>97% 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 ability to neutralize Activin-mediated inhibition on MPC11 cell proliferation. The ED50 for this effect is typically 0.02-0.1 µg/mL in the presence of 10 ng/mL recombinant Activin A.2. Measured by its binding ability in a functional ELISA. 3. Immobilized human ACVR2B at 10 ug/mL (100 ul/well) can bind biotinylated human INHBA-His, The EC50 of biotinylated human INHBA-His is 0.112 ug/mL.4. 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.
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.