Recombinant Human Megalin/LRP-2 (C3) Protein, CF

Recombinant Human Megalin/LRP-2 (C3) Protein, CF Summary

Product Specifications

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.

Background: Megalin/LRP2

Megalin, also known as the low-density lipoprotein receptor-related protein 2 (LRP2), is a large type I transmembrane cell surface protein. This glycoprotein is a multi‑ligand endocytic receptor that is expressed in many different tissues but primarily in absorptive epithilial tissues such as the kidney (1). The Megalin protein is critical for the reuptake of numerous ligands, including lipoproteins, sterols, vitamin-binding proteins, and hormones. This protein also has a role in cell-signaling. Mutations in this gene cause Donnai-Barrow Syndrome (DBS) and Facio-Oculoacoustico-Renal Syndrome (FOAR) (1). Megalin is consisting of a 25 amino acid (aa) probable N‑terminal signal peptide sequence, a 4400 aa extracellular region, a 22 aa single transmembrane domain, and a 213 aa C‑terminal cytoplasmic tail. The entire extracellular region is made up of 36 class A motifs of putative ligand-binding domains arranged in four distinct clusters, 16 growth factor repeats separated by 8 YWTD spacer regions, and 1 epidermal growth factor-like repeat (2). The extracellular ligand-binding-domains bind diverse macromolecules including albumin, apolipoproteins B and E, and lipoprotein lipase (3). The amino acid 2698-3110 encodes the third class A motif cluster in human Megalin, termed Megalin C3. Human Megalin C3 shares 77% and 74% identity with mouse and rat Megalin C3.

Related Research Areas

• Blood-brain Barrier Transporters
• Glucose Homeostasis
• Lipoprotein Receptors and Associated Proteins
• Monocyte Markers
• Obesity
• Renal Markers
• Renin-Angiotensin System
• Scavenger Receptors
• Transport of Amyloid beta Across the Blood-Brain Barrier
• Uptake and Transport Molecules in VSMC
• Uptake of Amyloid beta by Glia Cells
• Vasoactive Peptide Hormones and Regulators
• Wnt Receptors