Leptin Mouse

Leptin Mouse Recombinant
Cat. No.
BT20872
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 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.
Shipped with Ice Packs
In Stock

Description

Leptin Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 147 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 peptide hormone primarily produced by white adipocytes. It plays a crucial role in regulating energy balance and food intake by signaling the status of energy stores to the brain.
Description
Recombinant Mouse Leptin, expressed in E. coli, is a non-glycosylated polypeptide chain consisting of 147 amino acids. With a molecular weight of 16 kDa, it is purified using proprietary chromatographic techniques to ensure high purity.
Physical Appearance
White, lyophilized (freeze-dried) powder, sterile filtered.
Formulation
The lyophilized Mouse Leptin is provided in a solution containing 0.0045mM NaHCO3 at a concentration of 1mg/ml.
Solubility
For reconstitution, it is recommended to dissolve the lyophilized Leptin in sterile 18MΩ-cm H2O to a concentration of at least 100µg/ml. This solution can be further diluted in other aqueous solutions as needed.
Stability
Lyophilized Leptin remains stable at room temperature for up to 3 weeks; however, for long-term storage, it is recommended to store it desiccated below -18°C. After reconstitution, store Leptin at 4°C for 2-7 days. For prolonged storage, freeze at -18°C after adding a carrier protein (0.1% HSA or BSA). Avoid repeated freeze-thaw cycles.
Purity
The purity of the Leptin is greater than 95.0%, as determined by: (a) Gel filtration analysis. (b) SDS-PAGE analysis.
Biological Activity
The biological activity of Mouse Leptin is assessed by its ability to stimulate the proliferation of BAF/3 cells, which are stably transfected with the long form of the human leptin receptor.
Protein Content
Protein concentration is determined using UV spectroscopy at 280 nm. An absorbance value of 0.20 is used as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated using the PC GENE computer analysis program for protein sequences (IntelliGenetics).
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Source
Escherichia Coli.
Amino Acid Sequence

AVPIQKVQDD TKTLIKTIVT RINDISHTQS VSAKQRVTGL DFIPGLHPIL SLSKMDQTLA VYQQVLTSLP SQNVLQIAND LENLRDLLHL LAFSKSCSLP QTSGLQKPES LDGVLEASLY STEVVALSRL QGSLQDILQQ LDVSPEC.

Product Science Overview

Discovery and Genetic Background

Leptin was first identified in 1994 through the cloning of the mouse and human leptin genes . The protein product of the obese gene, leptin, was found to be a key regulator of energy balance. Mice with mutations in the obese gene that block the synthesis of leptin exhibit obesity, diabetes, reduced activity, decreased metabolism, and lower body temperature .

Biological Functions

Leptin is primarily synthesized and secreted by white adipose tissue (WAT), which is now recognized as an active endocrine organ. WAT secretes a variety of hormones, collectively known as adipokines or adipocytokines, which have autocrine, paracrine, or endocrine effects on metabolic processes both in the periphery and the central nervous system (CNS) .

Initially considered an anti-obesity hormone due to its role in maintaining body weight, leptin has since been found to have significant effects on glycemic control and cognitive function . Leptin deficiency (hypoleptinemia) and leptin resistance (hyperleptinemia) are characterized by dysfunctional leptin signaling, leading to systemic metabolic defects, including obesity and diabetes .

Recombinant Leptin

Recombinant mouse leptin is produced using E. coli expression systems. The recombinant protein is often used in research to study leptin’s role in various physiological processes. It is typically purified to a high degree, with a purity of over 97% as determined by SDS-PAGE under reducing conditions . The endotoxin level is kept below 1.0 EU per 1 μg of protein, ensuring its suitability for biological assays .

Applications in Research

Recombinant leptin is used in various research applications, including cell proliferation assays, where it has been shown to stimulate the proliferation of BaF3 mouse pro-B cells transfected with human leptin receptors . It is also used to study the effects of leptin on energy balance, metabolism, and cognitive function .

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