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Recombinant Human Leptin R Fc Chimera Protein, CF

Catalog # 389-LR/CF | R&D Systems, Inc. a Bio-Techne Brand
Catalog #
Size / Price

Key Product Details

Accession #



Structure / Form

Disulfide-linked homodimer





Product Specifications


Mouse myeloma cell line, NS0-derived human Leptin R protein
Human Leptin R
Accession # P48357.2
6-His tag
N-terminus C-terminus


>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis


Predicted Molecular Mass

121 kDa (monomer)


155-175 kDa, under reducing conditions.


Measured by its ability to inhibit Leptin-dependent proliferation of BaF3 mouse pro‑B cells transfected with human Leptin R.
The ED50 for this effect is 0.02-0.12 µg/mL in the presence of 3 ng/mL Recombinant Human Leptin/OB (Catalog # 398-LP).

Formulation, Preparation and Storage

Formulation Lyophilized from a 0.2 μm filtered solution in MES, NaCl and CHAPS.
Reconstitution Reconstitute at 200 μg/mL in sterile 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.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: Leptin R

The Leptin receptor (Leptin R, gene name LEPR), also called OB R (obesity receptor), is a 150 kDa protein that is a member of the Class I cytokine receptor family. It mediates the activities of Leptin, a multi-functional hormone produced primarily by adipose tissues that plays roles in food intake, energy metabolism, angiogenesis, reproduction, hematopoiesis, bone metabolism, and immune function (1-3). The human Leptin R gene encodes 1165 amino acids (aa) including a signal peptide, an extracellular region with cytokine receptor homology (CRH), multiple fibronectin type III domains and a WSXWS motif, a transmembrane domain, and a cytoplasmic domain that supports JAK/STAT signaling (2, 3). Human Leptin R shares 76% aa sequence identity with mouse and rat Leptin R, and 83-86% with bovine, canine, equine and porcine Leptin R. Leptin R isoforms include a long form, OB RL or OB Rb (primary signaling form), and at least four shorter isoforms with truncated cytoplasmic domains, named OB Ra (ubiquitous), Rc, Rd, and Rf (2, 4). A soluble isoform, OB Re, is found in rodents but not humans (5). However, both humans and rodents produce soluble Leptin R due to release of soluble ectodomains by metalloproteinases such as ADAM10 (5, 6). OB Rb is highly expressed in the hypothalamus and mediates the anti-orexigenic effects of Leptin (1, 2). Mutations of ObRb have caused extreme obesity in humans, mice (db/db “diabetes”), and rats (Zucker fa/fa “fatty”) (1, 7-9). Shorter isoforms of Leptin R exhibit limited signaling capability, but mediate endocytosis and degradation of Leptin and passage through the blood-brain barrier (4, 5, 10, 11). Soluble Leptin R is the primary Leptin-binding protein in blood, where it maintains a pool of available bioactive Leptin, delays Leptin clearance from circulation, and down-regulates blood-brain transmission of Leptin (5-7, 10). In humans, soluble Leptin R levels are inversely proportional to adiposity and are elevated in females versus males (12). Soluble Leptin R is also found up-regulated in patients with chronic heart failure, end-stage renal disease, and anorexia (13-15). It is expressed by tumor-initiating stem cells, and is proposed as a link between between cancer and obesity (16).


  1. Israel, D. and S. Chua, Jr. (2010) Trends Endocrinol. Metab. 21:10.
  2. Oswal, A. and G. Yeo (2010) Obesity 18:221.
  3. Tartaglia, L.A. et al. (1995) Cell 83:1263.
  4. Murakami, T. et al. (1997) Biochem. Biophys. Res. Commun. 231:26.
  5. Lou, P.H. et al. (2010) PLoS ONE 5:e11669.
  6. Schaab, M. et al. (2012) PLoS ONE 7:e34787.
  7. Huang, L. et al. (2001) J. Biol. Chem. 276:6343.
  8. Chen, H. et al. (1996) Cell 84:491.
  9. Phillips, M.S. et al. (1996) Nature Genet. 13:18.
  10. Tu, H. et al. (2008) J. Cell Physiol. 214:301.
  11. Tu, H. et al. (2007) J. Cell. Physiol. 212:215.
  12. Mann, D.R. et al. (2003) J. Clin. Endocrinol. Metab. 88:3339.
  13. Schulze, P.C. et al. (2003) Eur. J. Heart Fail. 5:33.
  14. Pecoits-Filho, R. et al. (2002) Eur. J. Clin. Invest. 32:811.
  15. Krizova, J. et al. (2002) Endocr. Res. 28:199.
  16. Feldman, D.E. et al. (2012) Proc. Natl. Acad. Sci. USA 109:829.

Long Name

Leptin Receptor

Alternate Names

B219, CD295, LEPR, LeptinR, OB R

Entrez Gene IDs

3953 (Human); 16847 (Mouse)

Gene Symbol



Product Documents for Recombinant Human Leptin R Fc Chimera Protein, CF

Certificate of Analysis

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Product Specific Notices for Recombinant Human Leptin R Fc Chimera Protein, CF

For research use only

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