Leptin Ovine

Leptin Ovine Recombinant
Cat. No.
BT21043
Source
Escherichia Coli.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Leptin Ovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.
The Leptin is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Leptin is a 16-kDa hormone produced by white adipose tissue that plays a crucial role in regulating food intake and energy balance by signaling the brain about the body's fat stores.
Description
Recombinant Ovine Leptin, expressed in E. coli, is a single-chain polypeptide consisting of 146 amino acids. This non-glycosylated protein has a molecular weight of 16 kDa and is purified using proprietary chromatographic techniques.
Physical Appearance
White, lyophilized (freeze-dried) powder, sterile filtered.
Formulation
The protein was lyophilized from a solution containing 1mg/ml protein and 0.0045mM NaHCO3.
Solubility
To reconstitute the lyophilized Leptin, dissolve it in sterile 18 MΩ-cm H2O to a concentration of at least 100 µg/ml. The reconstituted solution can then be diluted further with other aqueous solutions.
Stability
Lyophilized Leptin remains stable for 3 weeks at room temperature but should be stored desiccated below -18°C for optimal preservation. After reconstitution, store Leptin at 4°C for 2-7 days. For long-term storage, freezing below -18°C is recommended. To enhance stability during long-term storage, consider adding a carrier protein (0.1% HSA or BSA). Avoid repeated freeze-thaw cycles.
Purity
The purity is determined to be greater than 95.0% using the following methods: (a) Size Exclusion-High Performance Liquid Chromatography (SEC-HPLC) analysis and (b) Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) analysis.
Biological Activity
The biological activity of this product is confirmed by its ability to stimulate the proliferation of BAF/3 cells stably expressing the long form of the human leptin receptor.
Protein Content
Protein concentration is determined using two independent methods: 1) UV spectroscopy at 280 nm, employing an extinction coefficient of 0.2 for a 0.1% (1mg/ml) solution, calculated using the PC GENE computer analysis program (IntelliGenetics). 2) Reverse Phase-High Performance Liquid Chromatography (RP-HPLC), using a calibrated solution of Ovine Leptin as a reference standard.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Source
Escherichia Coli.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.

Product Science Overview

Structure and Production

Leptin ovine recombinant, often referred to as roLeptin, is a recombinant form of leptin derived from sheep. It is produced in Escherichia coli (E. coli) and is a single, non-glycosylated polypeptide chain consisting of 146 amino acids. The molecular mass of leptin ovine recombinant is approximately 16 kDa . The production process involves proprietary chromatographic techniques to ensure high purity and quality.

Mechanism of Action

Leptin exerts its effects by binding to the leptin receptor (LEPR), which is primarily located in the hypothalamus of the brain. Upon binding to its receptor, leptin activates several intracellular signaling pathways that regulate appetite and energy expenditure. The majority of LEPR is localized in intracellular compartments, including the endoplasmic reticulum, trans-Golgi apparatus, and endosomes, with only a minor fraction present at the plasma membrane .

Biological Functions

Leptin plays a vital role in various physiological processes, including:

  • Regulation of Food Intake: Leptin inhibits appetite by signaling to the brain that the body has sufficient energy stores, thereby reducing food intake.
  • Energy Expenditure: Leptin increases energy expenditure by promoting the oxidation of fatty acids and enhancing thermogenesis.
  • Reproductive Function: Leptin is involved in the regulation of reproductive function by influencing the hypothalamic-pituitary-gonadal axis.
  • Immune Function: Leptin modulates immune responses by affecting the production and activity of various immune cells.
Clinical Significance

Leptin has significant clinical implications, particularly in the context of obesity and metabolic disorders. Individuals with congenital leptin deficiency or mutations in the LEPR gene exhibit severe early-onset obesity and hyperphagia (excessive eating). Leptin replacement therapy has been shown to be effective in treating these conditions by restoring normal appetite and energy balance .

However, the majority of obese individuals do not have mutations in the leptin or LEPR genes but often exhibit elevated circulating levels of leptin, a condition known as leptin resistance. This condition is characterized by the body’s inability to respond to leptin’s signals, leading to continued overeating and weight gain. Understanding the molecular mechanisms underlying leptin resistance remains a significant challenge in obesity research .

Research and Applications

Recombinant leptin, including leptin ovine recombinant, is widely used in research to study its physiological and biochemical effects. It is also utilized in various experimental models to investigate the mechanisms of leptin signaling and resistance. Additionally, leptin has potential therapeutic applications in treating metabolic disorders, obesity, and related conditions.

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