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Recombinant Mouse Leptin R Fc Chimera Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Mouse Leptin R Fc Chimera Protein, CF Summary

Details of Functionality
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 2-10 ng/mL in the presence of 1 ng/mL recombinant mouse Leptin.
Source
Mouse myeloma cell line, NS0-derived mouse Leptin R protein
Mouse Leptin R
(Leu22-Gly839)
Accession # P48356
IIEGRMDP Mouse IgG2A
(Glu98-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Leu22
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
Lepr
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
119.6 kDa (monomer).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
125-190 kDa, reducing conditions

Packaging, Storage & Formulations

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.
Buffer
Lyophilized from a 0.2 μm filtered solution in MES and NaCl.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse Leptin R Fc Chimera Protein, CF

  • B219
  • CD295 antigen
  • CD295
  • DB
  • DKFZp686B1731
  • huB219
  • LEPR
  • LEP-R
  • Leptin R
  • leptin receptor
  • LeptinR
  • OB R
  • OB receptor
  • OB-R
  • OBRCD295

Background

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 mouse Leptin R gene encodes 1162 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). Mouse Leptin R shares 93% aa sequence identity with rat Leptin R and 74‑76% with human, 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 rodents and humans 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.

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Bioinformatics

Gene Symbol Lepr
Uniprot