Recombinant Human LRP-6 Protein, Active

Beta LifeScience SKU/CAT #: BLK-03329P
Human LRP-6 on Bis-Tris PAGE under reduced condition. The purity is greater than 90%.
Human LRP-6 on Bis-Tris PAGE under reduced condition. The purity is greater than 90%.

Recombinant Human LRP-6 Protein, Active

Beta LifeScience SKU/CAT #: BLK-03329P
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

Description Recombinant Human LRP-6 Protein is expressed from HEK293 with mFc (IgG2a) tag at the C-terminus.It contains Ala20-Pro630.
Gene Background Low-density lipoprotein receptor protein 6 (LRP6) is a Wnt co-receptor with essential functions in the Wnt/β-catenin pathway, and mutations in LRP6 gene are linked to many complex human diseases, including metabolic syndrome, cancer, Alzheimer's disease and osteoporosis. LRP-6 interacts closely with PDGF receptor β and TGF-β receptor 1 at the cell membrane, suggesting that it may have roles in pathways other than WNT/β-catenin.
Accession O75581-1
Target Symbol LRP-6
Synonyms LRP-6; DCAD2; FLJ90062; FLJ90421;LRP6
Species Human
Expression System Mammalian Cell
Purity > 90% as determined by Bis-Tris PAGE
Tag C-mFc
Expression Range Ala20-Pro630
Mol. Weight The protein has a predicted MW of 95.32 kDa. Due to glycosylation, the protein migrates to 97-110 kDa based on Bis-Tris PAGE result.
Form Liquid
Formulation Supplied as 0.22 um filtered solution in PBS (pH 7.4).
Endotoxin Less than 1 EU per ug by the LAL method.
Activity Immobilized Human DKK1, His Tag at 5ug/ml (100ul/well) on the plate. Dose response curve for Human LRP-6, mFc Tag with the EC50 of 1.03ug/ml determined by ELISA (QC Test).
Biotinylated No
Shipping Shipped with dry ice.
Storage Valid for 12 months from date of receipt when stored at -80°C.; Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize 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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