Recombinant Human LRP-5-Protein, Active
Beta LifeScience
SKU/CAT #: BLK-00929P-100UG

Human LRP-5 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.
Recombinant Human LRP-5-Protein, Active
Beta LifeScience
SKU/CAT #: BLK-00929P-100UG
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.
Product Overview
Description | Recombinant Human LRP-5-Protein is expressed from HEK293 with hFc tag at the C-Terminus.It contains Glu644-Gln1263. |
Purity | > 95% as determined by Tris-Bis PAGE |
Accession | O75197 |
Target Symbol | LRP-5 |
Species | Human |
Expression System | HEK293 |
Tag | C-hFc |
Expression Range | Glu644-Gln1263 |
Mol. Weight | The protein has a predicted MW of 96.51 kDa. Due to glycosylation, the protein migrates to 100-115 kDa based on Tris-Bis PAGE result. |
Form | Liquid |
Formulation | Supplied as 0.22um filtered solution in PBS, 100mM L-arginine (pH 7.4). |
Endotoxin | Less than 1EU per ug by the LAL method. |
Activity | Immobilized Human DKK1, His Tag at 2ug/ml (100ul/well) on the plate. Dose response curve for Human LPR-5, hFc Tag with the EC50 of 1.04ug/ml determined by ELISA (QC Test). The affinity constant of 0.28 uM as determined in SPR assay (Biacore T200). Contact us for detailed testing images. |
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. |
Shipping | Shipped with dry ice. |
Gene Background | A role for low-density lipoprotein-related receptor 5 (LRP5) in human bone was first established by the identification of genetic alterations that led to dramatic changes in bone mass. Shortly thereafter, mutations that altered the function of the sclerostin (SOST) gene were also associated with altered human bone mass. Subsequent studies of LRP5 and sclerostin have provided important insights into the mechanisms by which these proteins regulate skeletal homeostasis. |