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Recombinant Mouse Leptin R Fc Chimera Protein

Catalog #: 497-LR
11 Citations Datasheet / COA / SDS

Carrier Free

Catalog # Availability Size / Price Qty
497-LR-100/CF

With Carrier

Catalog # Availability Size / Price Qty
497-LR-100
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Citations (11)
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Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Mouse Leptin R Fc Chimera Protein Summary

Product Specifications

Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
Activity
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 0.004-0.015 µg/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
(Ala20-Gly839)
Accession # Q3US58		 IIEGRDMD Human IgG1
(Pro100-Lys330)		 6-His tag
N-terminus C-terminus
Accession #
Q3US58
N-terminal Sequence
Analysis
Ala20
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
120 kDa (monomer)
SDS-PAGE
150-170 kDa, reducing conditions

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497-LR (with carrier)

Product Datasheet
COA
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497-LR/CF (carrier free)

Product Datasheet
COA
SDS

Carrier Free

What does CF mean?

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.

What formulation is right for me?

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.

497-LR

Formulation Lyophilized from a 0.2 μm filtered solution in MES, NaCl and CHAPS with BSA as a carrier protein.
Reconstitution Reconstitute at 200 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
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.

497-LR/CF

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.
Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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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 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).

References
  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
Entrez Gene IDs
3953 (Human); 16847 (Mouse)
Alternate Names
B219; CD295 antigen; CD295; DB; DKFZp686B1731; huB219; LEPR; LEP-R; Leptin R; leptin receptor; LeptinR; OB R; OB receptor; OB-R; OBRCD295

Citations for Recombinant Mouse Leptin R Fc Chimera Protein

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.

11 Citations: Showing 1 - 10
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  1. Enhancing Oral Delivery of Biologics: A Non-Competitive and Cross-Reactive Anti-Leptin Receptor Nanofitin Demonstrates a Gut-Crossing Capacity in an Ex Vivo Porcine Intestinal Model
    Authors: Masloh, S;Chevrel, A;Culot, M;Perrocheau, A;Kalia, YN;Frehel, S;Gaussin, R;Gosselet, F;Huet, S;Zeisser Labouebe, M;Scapozza, L;
    Pharmaceutics
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  2. Epiregulin as an Alternative Ligand for Leptin Receptor Alleviates Glucose Intolerance without Change in Obesity
    Authors: NJ Song, A Lee, R Yasmeen, Q Shen, K Yang, SB Kumar, D Muhanna, S Arnipalli, SF Noria, BJ Needleman, JW Hazey, DJ Mikami, J Ortega-Ana, R Jiménez-Fl, J Prokop, O Ziouzenkov
    Cells, 2022-01-26;11(3):.
    Species: Mouse
    Sample Types: Recombinant Proteins
    Applications: Bioassay
  3. Primary cilia mediate early life programming of adiposity through lysosomal regulation in the developing mouse hypothalamus
    Authors: CH Lee, DK Song, CB Park, J Choi, GM Kang, SH Shin, I Kwon, S Park, S Kim, JY Kim, H Dugu, JW Park, JH Choi, SH Min, JW Sohn, MS Kim
    Nat Commun, 2020-11-13;11(1):5772.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  4. Fructose promotes cytoprotection in melanoma tumors and resistance to immunotherapy
    Authors: LM Kuehm, N Khojandi, A Piening, LE Klevorn, SC Geraud, NR McLaughlin, K Griffett, TP Burris, KD Pyles, AM Nelson, ML Preuss, KA Bockerstet, MJ Donlin, KS McCommis, RJ DiPaolo, RM Teague
    Cancer Immunol Res, 2020-10-06;0(0):.
    Species: Mouse
    Sample Types: In Vivo
    Applications: Bioassay
  5. Leptin receptor signaling in T cells is required for Th17 differentiation.
    Authors: Reis B, Lee K, Fanok M, Mascaraque C, Amoury M, Cohn L, Rogoz A, Dallner O, Moraes-Vieira P, Domingos A, Mucida D
    J Immunol, 2015-04-27;194(11):5253-60.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  6. Leptin exacerbates sepsis-mediated morbidity and mortality.
    Authors: Shapiro NI, Khankin EV, van Meurs M
    J. Immunol., 2010-06-02;185(1):517-24.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  7. Soluble receptor inhibits leptin transport.
    Authors: Tu H, Kastin AJ, Hsuchou H, Pan W
    J. Cell. Physiol., 2008-02-01;214(2):301-5.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  8. High circulating leptin receptors with normal leptin sensitivity in liver-specific insulin receptor knock-out (LIRKO) mice.
    Authors: Cohen SE, Kokkotou E, Biddinger SB, Kondo T, Gebhardt R, Kratzsch J, Mantzoros CS, Kahn CR
    J. Biol. Chem., 2007-06-07;282(32):23672-8.
    Applications: ELISA (Standard)
  9. Leptin neutralization interferes with pathogenic T cell autoreactivity in autoimmune encephalomyelitis.
    Authors: De Rosa V, Procaccini C, La Cava A, Chieffi P, Nicoletti GF, Fontana S, Zappacosta S, Matarese G
    J. Clin. Invest., 2006-01-12;116(2):447-55.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  10. BiaCore analysis of leptin-leptin receptor interaction: evidence for 1:1 stoichiometry.
    Authors: Mistrik P, Moreau F, Allen JM
    Anal. Biochem., 2004-04-15;327(2):271-7.
    Species: Human, Mouse, Rat
    Sample Types: Recombinant Protein
    Applications: Surface Plasmon Resonance
  11. Antiangiogenic and antitumor efficacy of EphA2 receptor antagonist.
    Authors: Dobrzanski P, Hunter K, Jones-Bolin S, Chang H, Robinson C, Pritchard S, Zhao H, Ruggeri B
    Cancer Res., 2004-02-01;64(3):910-9.
    Species: Rat
    Sample Types: Whole Cells
    Applications: Bioassay

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