Leptin Protein, Human

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Based on 3 publication(s) in Google Scholar

Leptin is a cytokine-like sugar secretory protein secreted by adipocytes that helps regulate energy balance by inhibiting food intake and increasing thermogenesis. Leptin can activate the JAK2-STAT3 and PI3K-AKT/mTOR pathways to regulate energy metabolism, prolong the QT interval via MAPK in the myocardium, and play a protective role in the gastric mucosa by inducing NO/CGRP release via the vagus nerve. Circulating CRP protein binds to leptin and blocks signal transduction, leading to obesity resistance. Leptin Protein, Human is a recombinant human Leptin protein expressed by E. coli without a tag.

For research use only. We do not sell to patients.
  • Species: Human
  • Source: E. coli
  • Storage:
    Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
  • Biological Activity
  • Technical Parameters
  • Product Properties
  • Documentation
  • References
  • Help & FAQs

Biological Activity

Description

Leptin is a cytokine-like sugar secretory protein secreted by adipocytes that helps regulate energy balance by inhibiting food intake and increasing thermogenesis. Leptin can activate the JAK2-STAT3 and PI3K-AKT/mTOR pathways to regulate energy metabolism, prolong the QT interval via MAPK in the myocardium, and play a protective role in the gastric mucosa by inducing NO/CGRP release via the vagus nerve. Circulating CRP protein binds to leptin and blocks signal transduction, leading to obesity resistance. Leptin Protein, Human is a recombinant human Leptin protein expressed by E. coli without a tag.

Background

Leptin is a hormone secreted by adipocytes that helps regulate energy balance by inhibiting food intake and increasing thermogenesis. It belongs to the cytokine-like protein family. Leptin has a conserved four-helix bundle conformation, with a tertiary structure stabilized by disulfide bonds. It lacks a classical signal peptide but is secreted via a non-classical pathway. The C-terminal domain of leptin mediates receptor binding, while the N-terminal region promotes oligomerization. Leptin binds to the long receptor OB-Rb in hypothalamic neurons and peripheral tissues, activating the JAK2-STAT3 and PI3K-AKT/mTOR pathways, inhibiting food intake and enhancing energy expenditure. In cardiomyocytes, leptin mediates MAPK activation through OB-Rb, reducing heart rate and prolonging the QT interval, an effect that is independent of β-adrenergic signaling[1][2][3][4].
In the gastric mucosa, leptin stimulates sensory neurons to release NO and CGRP via the vagus nerve, enhancing blood flow and protecting tissues from ischemia-reperfusion injury. Circulating C-reactive protein (CRP) binds to leptin, blocks receptor interaction and attenuates STAT3 phosphorylation, leading to leptin resistance in obesity[3][4]. Upstream regulators of leptin include leptin secreted by adipocytes and CRP synthesized by the liver; downstream targets include STAT3, PI3K, eNOS and mTOR, which play a role in regulating metabolism, neurogenesis and vascular function[1][4].
In metabolic diseases, leptin resistance is associated with hyperleptinemia and inhibition of CRP-mediated signaling, and leptin supplementation may inhibit congenital lipodystrophy and type 2 diabetes[4]. At the same time, Leptin's direct effect on cardiac repolarization (QT interval prolongation) and its interaction with CRP may be involved in obesity-related arrhythmias and atherosclerosis[2]. Leptin also enhances gastric mucosal blood flow and protects against ischemic damage through vagus-sensory nerve-mediated NO/CGRP release, and can be used in the study of peptic ulcer disease[3].

Verified Bioactivity

1.The ED50 as determined by a chemotaxis bioassay using human Leptin R transfected BaF3 murine proB cells is less than 2.0 ng/mL, corresponding to a specific activity of > 5.0 × 105 IU/mg.
2.Immobilized Mouse LEPR (C-10His) at 10 μg/mL (100 μL/well) can bind Leptin, Human. The ED50 is 17.15 ng/mL.
3.Measured in a cell proliferation assay using BaF3 mouse pro-B cells transfected with human Leptin R. The ED50 for this effect is ≤1.948 ng/mL, corresponding to a specific activity is ≥5.133×105 units/mg.
4. Immobilized Recombinant Mouse LEPR (C-10His) at 2 μg/mL(100 μl/well) can bind Recombinant Human Leptin: Biotinylated by NHS-biotin prior to testing. The ED50 of Recombinant Human Leptin is 3.85 ng/mL.

Results
  • Experimental Validation Results for Leptin Protein, Human
    Measured in a cell proliferation assay using BaF3 mouse pro-B cells transfected with human Leptin R. The ED50 for this effect is 1.948 ng/mL, corresponding to a specific activity is 5.133×105 units/mg.

Technical Parameters

  • Species Human
  • Source E. coli
  • Tag Tag Free
  • Accession
  • Gene ID
  • Molecular Construction
    • N-term
    • Leptin (V22-C167)
      Accession # P41159
    • C-term
  • Protein Length

    Full Length of Mature Protein

  • Synonyms

    rHuLeptin; Obesity protein; OB

  • AA Sequence

    VPIQKVQDDTKTLIKTIVTRINDISHTQSVSSKQKVTGLDFIPGLHPILTLSKMDQTLAVYQQILTSMPSRNVIQISNDLENLRDLLHVLAFSKSCHLPWASGLETLDSLGGVLEASGYSTEVVALSRLQGSLQDMLWQLDLSPGC

  • Molecular Weight

    Approximately 14 kDa, based on SDS-PAGE under reducing conditions.

  • Purity

    ≥ 95%, as determined by reducing SDS-PAGE.

    • Experimental Validation Results for Leptin Protein, Human
      ≥ 95%, as determined by reducing SDS-PAGE.

Product Properties

Appearance

Lyophilized powder

Formulation

1. Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 8% trehalose.
2. Lyophilized from a 0.22 μm filtered solution of 20 mM Tris-HCl, 50 mM NaCl, 10% Trehalose, 0.02% Tween 80, pH 8.5.
Note: If this product is used in SPR assay, please note that the protein buffer should not contain primary amino components (such as Tris and Imidazole), and the buffer needs to be replaced.

Endotoxin Level

<1 EU/μg, determined by LAL method.

Reconstitution

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Storage & Stability

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Shipping

Room temperature in continental US; may vary elsewhere.

References

Calculators

Reconstitution Calculator

Volume (to add to vial) = Mass (in vial) ÷ Desired Reconstitution Concentration

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Desired Reconstitution Concentration Desired Reconstitution Concentration
Dilution Calculator

Concentration (start) × Volume (start) = Concentration (final) × Volume (final)

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The Specific Activity Calculator Equation
  • Specific Activity (Unit/mg)
  • Biological Activity (ED50)

Specific Activity (Unit/mg) = 106 ÷ Biological Activity (ED50)

Specific Activity (Unit/mg) Specific Activity (Unit/mg)
Unit/mg
= 106 ÷
Biological Activity (ED50) Biological Activity (ED50)
106 ÷
ng/mL
MOQ
Minimum order quantity
100 mg

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