Recombinant Mouse LRP-4 His-tag Protein, CF Summary
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 100 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
When Recombinant Mouse USAG1 (Catalog # 9008-SD) is used at 2 μg/mL (100 μL/well), it binds to Recombinant Mouse LRP-4 (Catalog # 10229-LR) with an ED50 of 80-800 ng/mL.
2 μg/lane of Recombinant Mouse LRP-4 His-tag was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 180-235 kDa.
LDL receptor-related protein 4 (LRP-4), also known as Megf7, is an approximately 220 kDa type I membrane protein in the LDL receptor superfamily. LRP-4 plays an important role in development of the neuromuscular junction (NMJ), bones, teeth, mammary placodes, and hair follicles (1, 2). Mature mouse LRP-4 consists of a 1705 amino acid (aa) extracellular domain (ECD), a 21 aa transmembrane segment, and a 159 aa cytoplasmic domain. The ECD contains 3 EGF-like domains, 8 LDLR-A domains, and 20 LDLR-B repeats that fold into 4 beta-propeller domains (3, 4). Within the ECD, mouse LRP-4 shares 97% and 99% aa sequence identity with human and rat LRP-4, respectively. The ECD of LRP-4 can be shed by ADAM10 mediated cleavage (5). LRP-4 is expressed on myotubes (6, 7), neurons (8, 9), osteocytes and osteoblasts (10, 11), developing tooth epithelium (12), and male and female germ cells (13). It is localized to NMJ on developing myotubes, and it associates in cis with the muscle-specific kinase MuSK (6, 7). Its binding to neuron-derived Agrin promotes additional LRP-4 association with MuSK, MuSK activation, clustering of AChR, and postsynaptic development of the NMJ (6, 7, and 14). LRP-4 also enhances presynaptic differentiation of the NMJ, although this does not require Agrin (14). Neuronal LRP-4 additionally binds ApoE and Fspondin (8, 9). LRP-4 regulates both BMP and Wnt signaling through binding to Wise, Sclerostin, and Dkk1 (10, 12). These interactions are important for the control of bone growth and mineralization, tooth morphogenesis, and the development of mammary placodes, hair follicles, and whiskers (10, 12, and 15).
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