Recombinant Mouse ALK-1 Protein (His & Fc Tag)

Beta LifeScience SKU/CAT #: BLPSN-0139

Recombinant Mouse ALK-1 Protein (His & Fc Tag)

Beta LifeScience SKU/CAT #: BLPSN-0139
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Product Overview

Tag His&Fc
Host Species Mouse
Accession NP_033742.2
Synonym Acvrlk1, AI115505, AI427544, Alk1
Background Activin A receptor, type II-like 1 (ACVRL1), also known as ALK-1 (activin receptor-like kinase 1), is an endothelial-specific type I receptor of the TGF-beta (transforming growth factor beta) receptor family of ligands. On ligand binding, a heteromeric receptor complex forms consisting of two type II and two type I transmembrane serine/threonine kinases. ACVRL1 protein is expressed in certain blood vessels of kidney, spleen, heart and intestine, serving as an important role during vascular development. Mutations in ACVRL1 gene are associated with hemorrhagic telangiectasia type 2, also known as Rendu-Osler-Weber syndrome 2 and vascular disease.
Description A DNA sequence encoding the mouse ALK1 (NP_033742.2) precursor (Met 1-Pro 119) was fused with the C-terminal His-tagged Fc region of human IgG1 at the C-terminus.
Source HEK293
Predicted N Terminal Asp 23
AA Sequence Met 1-Pro 119
Molecular Weight The secreted recombinant mouse ALK1/Fc is a disulfide-linked homodimer after removal of the signal peptide. The reduced monomer comprises 345 a.a. with a predicted molecular mass of 39 kDa. As a result of glycosylation, it migrates as an approximately 50-55 kDa band in SDS-PAGE under reducing conditions.
Purity >95% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Measured by its ability to inhibit BMP9-induced alkaline phosphatase production by MC3T3E1 mouse chondrogenic cells. David, L. et al. (2007) Blood 109:1953.The ED50 for this effect is typically 60-300 ng/mL in the presence of 2 ng/mL of recombiant human BMP9.
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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