Leptin Porcine

Leptin Porcine Recombinant
Cat. No.
BT21202
Source
Escherichia Coli.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(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.
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Description

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

Product Specs

Introduction
Leptin is a 16-kDa peptide hormone primarily produced by white adipocytes. It plays a crucial role in regulating food intake and energy balance by acting as a signaling molecule that conveys information about the body's fat stores to the brain.
Description
Recombinant Porcine Leptin, expressed in E. coli, is a non-glycosylated polypeptide chain consisting of 146 amino acids, with an additional alanine residue at the N-terminus. It has a molecular weight of 16 kDa and is purified using proprietary chromatographic techniques.
Physical Appearance
Sterile white powder obtained by lyophilization (freeze-drying).
Formulation
The lyophilized protein was prepared from a 1 mg/ml solution containing 0.02% sodium bicarbonate (NaHCO₃).
Solubility
To reconstitute the lyophilized recombinant porcine leptin, it is advised to dissolve it in sterile 0.4% NaHCO₃ solution adjusted to a pH of 8-9. The initial reconstitution concentration should be at least 100 µg/ml, which can be further diluted as needed in other aqueous solutions.
Stability
Lyophilized Leptin remains stable at room temperature for up to 3 weeks; however, it is recommended to store it desiccated below -18°C for long-term storage. After reconstitution, store Leptin at 4°C for 2-7 days. For extended storage, freeze at -18°C after adding a carrier protein like 0.1% HSA or BSA. Avoid repeated freeze-thaw cycles.
Purity
The purity is determined to be greater than 98.0% using the following methods: (a) Gel filtration analysis. (b) SDS-PAGE analysis.
Biological Activity
The biological activity is confirmed by the induction of proliferation in BAF/3 cells stably expressing the long form of the human leptin receptor.
Protein Content
Two independent methods were employed for protein quantification: 1. UV spectroscopy at 280 nm, utilizing an absorbance value of 0.57 as the extinction coefficient for a 0.1% (1 mg/ml) solution. This value is derived from the PC GENE computer analysis program for protein sequences (IntelliGenetics). 2. RP-HPLC analysis, employing a calibrated solution of Leptin Porcine 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-Trp.

Product Science Overview

Discovery and Function

Leptin was discovered in 1994 by Jeffrey Friedman and his colleagues at Rockefeller University. The hormone is encoded by the ob (obesity) gene and is secreted into the bloodstream, where it travels to the brain and binds to leptin receptors in the hypothalamus. This binding action signals the brain to reduce appetite and increase energy expenditure .

Recombinant Leptin

Recombinant leptin refers to leptin that is produced through recombinant DNA technology. This involves inserting the gene that encodes leptin into a host organism, such as bacteria (e.g., E. coli), which then produces the hormone. Recombinant leptin is used in research and therapeutic applications to study its effects and potential treatments for obesity and metabolic disorders .

Porcine Leptin

Porcine leptin is leptin derived from pigs. It shares a high degree of similarity with leptin from other species, including humans, making it a valuable model for studying leptin’s functions and effects. Porcine leptin has been extensively studied for its role in reproduction, energy metabolism, and fat regulation .

Applications and Research

Recombinant porcine leptin has been used in various research studies to understand its effects on different biological processes. For example, studies have shown that leptin can modulate steroidogenesis in porcine granulosa cells, which are involved in ovarian function and reproduction . Leptin’s role in energy homeostasis has also been explored, particularly in the context of obesity and metabolic disorders .

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