Leptin Dog
Leptin Dog Recombinant
Cat. No.
BT20363
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) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.
(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 Dog 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.
The Leptin is purified by proprietary chromatographic techniques.
Product Specs
Introduction
Leptin is a 16 kDa hormone primarily produced by adipocytes (fat cells) that plays a crucial role in regulating energy balance and food intake. It acts as a signaling molecule, informing the brain about the body's fat stores.
Description
Leptin Dog Recombinant is a non-glycosylated polypeptide chain containing 146 amino acids, with a molecular weight of 16 kDa. It is produced in E. coli and purified using specialized chromatographic techniques.
Physical Appearance
Sterile, white, lyophilized powder.
Formulation
The Leptin protein is lyophilized from a 0.02% NaHCO₃ solution at a concentration of 1 mg/ml.
Solubility
For reconstitution, it is recommended to dissolve the lyophilized Leptin in sterile 0.4% NaHCO₃ solution adjusted to a pH of 8-9, at a concentration not less than 100 µg/ml. This solution can then be further diluted with other aqueous solutions as needed.
Stability
Lyophilized Leptin remains stable at room temperature for up to 3 weeks; however, it is recommended to store it desiccated below -18°C. After reconstitution, Leptin should be stored at 4°C for short-term use (2-7 days) and below -18°C for long-term storage. For extended storage, adding a carrier protein like 0.1% HSA or BSA is advised. Avoid repeated freeze-thaw cycles.
Purity
The purity of Leptin is determined using the following methods and is found to be greater than 98.0%:
(a) Size Exclusion Chromatography-High Performance Liquid Chromatography (SEC-HPLC)
(b) Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE)
(a) Size Exclusion Chromatography-High Performance Liquid Chromatography (SEC-HPLC)
(b) Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE)
Biological Activity
The biological activity of Leptin is confirmed by its ability to stimulate the proliferation of BAF/3 cells, which have been stably transfected with the long form of the human leptin receptor.
Protein Content
Protein concentration is determined using UV spectroscopy at a wavelength of 280 nm. An extinction coefficient of 0.20 is used for a 0.1% (1 mg/ml) solution at pH 8.0. This value is calculated based on the protein sequence analysis using the PC GENE computer program (IntelliGenetics).
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 Function
Mechanism of Action
Leptin functions as a key afferent signal from fat cells in the feedback system that controls body fat stores . When fat stores increase, leptin levels rise, signaling the brain to reduce appetite and increase energy expenditure. Conversely, when fat stores decrease, leptin levels fall, leading to increased appetite and reduced energy expenditure .
Biological Roles
- Regulation of Food Intake and Energy Balance: Leptin helps maintain energy homeostasis by regulating hunger and metabolism .
- Thermogenesis: It influences the production of heat in the body, contributing to energy expenditure .
- Blood Glucose Regulation: Leptin plays a role in maintaining normal blood glucose levels .
- Endocrine Functions: It is involved in the regulation of immune and inflammatory responses, hematopoiesis (formation of blood cells), angiogenesis (formation of new blood vessels), and wound healing .
Clinical Significance
Recombinant Leptin in Research
Recombinant leptin, including dog recombinant leptin, is produced using genetic engineering techniques. It is expressed in systems such as E. coli to obtain the protein in a purified form . This recombinant protein is used in various research applications to study leptin’s physiological roles and potential therapeutic uses.
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