Recombinant Human LRP-4 Protein, CF Summary
Product Specifications
Human LRP-4 (Ser21-Ser1725) Accession # AAI36669 |
GGGSGGGSGGGS | 6-His |
N-terminus | C-terminus | |
Analysis
Product Datasheets
Carrier Free
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.
5948-LR
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 300 μg/mL in PBS. |
Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Reconstitution Calculator
Background: LRP-4
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 human 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, human LRP-4 shares 97% aa sequence identity with mouse and rat LRP-4. 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 post-synaptic development of the NMJ (6, 7, 14). LRP-4 also enhances presynaptic differentiation of the NMJ, although this does not require Agrin (14). Neuronal LRP-4 additionally binds ApoE and F-spondin (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, 15).
- Zong, Y. and R. Jin (2012) Cell. Mol. Life Sci. Nov 22 Epub.
- Ohazama, A. et al. (2010) Am. J. Med. Genet. A 152A:2974.
- Nakayama, M. et al. (1998) Genomics 51:27.
- Tomita, Y. et al. (1998) J. Biochem. 124:784.
- Dietrich, M.F. et al. (2010) PLoS ONE 5:e9960.
- Kim, N. et al. (2008) Cell 135:334.
- Zhang, B. et al. (2008) Neuron 60:285.
- Lu, Y. et al. (2007) Brain Res. 1177:19.
- Zisman, S. et al. (2007) J. Cell Biol. 178:1237.
- Leupin, O. et al. (2011) J. Biol. Chem. 286:19489.
- Choi, H.Y. et al. (2009) PLoS ONE 4:e7930.
- Ohazama, A. et al. (2008) PLoS ONE 3:e4092.
- Yamaguchi, Y.L. et al. (2006) Gene Expr. Patterns 6:607.
- Yumoto, N. et al. (2012) Nature 489:438.
- Ahn, Y. et al. (2013) Development 140:583.
Citations for Recombinant Human LRP-4 Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Neuronal MT1-MMP mediates ECM clearance and Lrp4 cleavage for agrin deposition and signaling in presynaptic development
Authors: MJ Oentaryo, AC Tse, CW Lee
J. Cell. Sci., 2020-08-05;0(0):.
Species: Xenopus
Sample Types: Whole Cells
Applications: Bioassay -
A Role of Agrin in Maintaining the Stability of Vascular Endothelial Growth Factor Receptor-2 during Tumor Angiogenesis
Authors: K Njah, S Chakrabort, B Qiu, S Arumugam, A Raju, AV Pobbati, M Lakshmanan, V Tergaonkar, G Thibault, X Wang, W Hong
Cell Rep, 2019-07-23;28(4):949-965.e7.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay
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