Leptin Rat, PEG

Pegylated Rat Leptin Recombinant
Cat. No.
BT21819
Source
Escherichia Coli.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 99.0% as determined by:
(a) Analysis by Gel-Filtration.
(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

Mono-Pegylated Leptin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 147 amino acids and an additional Ala at N-terminus having a molecular mass of 35.6 kDa (with 20 kDa PEG) as determined by mass spectometry. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Its half-life in circulation after SC injection was over 20 hours. Rat Leptin was purified by proprietary chromatographic techniques according to Salomon et al (2006) Protein Expression and Purification 47, 128–136 and then pegylated.

Product Specs

Introduction
Leptin, a 16-kDa peptide hormone primarily produced by white adipocytes, plays a crucial role in regulating energy balance and food intake. It serves as a critical messenger, conveying information about the body's fat stores to the central nervous system, thereby influencing appetite and metabolism.
Description
Recombinant Rat Leptin, mono-pegylated and produced in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 147 amino acids, with an additional alanine residue at the N-terminus. Mass spectrometry analysis reveals a molecular mass of 35.6 kDa, including the 20 kDa PEG moiety. Notably, due to its enhanced hydrodynamic volume, it exhibits a higher apparent molecular weight of 48 kDa on SDS-PAGE and elutes as an over 100 kDa protein in gel filtration (Superdex 200). Notably, its circulatory half-life after subcutaneous injection exceeds 20 hours. The purification of Rat Leptin was achieved using proprietary chromatographic methods, as described by Salomon et al. (2006) Protein Expression and Purification 47, 128-136. Subsequently, the purified protein underwent pegylation.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The protein was lyophilized from a 0.65 mg/ml solution containing 0.003 mM NaHCO3.
Solubility
For reconstitution of the lyophilized pegylated Rat Leptin, it is recommended to use sterile 0.4% NaHCO3 adjusted to pH 8.5. The reconstitution volume should be chosen to achieve a protein concentration of at least 100 µg/ml. This solution can be further diluted with other aqueous solutions as needed.
Stability
Lyophilized Rat Leptin demonstrates stability at room temperature for a period of 3 weeks; however, for long-term storage, it is advisable to store it desiccated at a temperature below -18°C. Upon reconstitution, Rat Leptin should be stored at 4°C for a period of 2-7 days. For extended storage, it is recommended to aliquot and store the reconstituted protein below -18°C. To ensure optimal stability during storage, the addition of a carrier protein (0.1% HSA or BSA) is recommended. Repeated freeze-thaw cycles should be avoided.
Purity
Purity exceeds 99.0% as determined by the following methods:
(a) Gel-Filtration analysis.
(b) SDS-PAGE analysis.
Biological Activity
Pegylated Rat Leptin exhibits the ability to stimulate the proliferation of BAF/3 cells that have been stably transfected with the long form of the human leptin receptor. Although its in vitro activity is slightly lower compared to the non-pegylated form, it demonstrates a substantial weight-reducing effect in vivo, primarily attributed to reduced food intake, surpassing the efficacy of non-pegylated leptin.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Source
Escherichia Coli.

Product Science Overview

Leptin: The Basics

Leptin is a 16 kDa protein that plays a critical role in regulating body weight, metabolism, and reproductive functions. It is encoded by the ob gene and is primarily produced in white adipose tissue. Leptin acts on receptors in the hypothalamus to suppress appetite and increase energy expenditure.

Recombinant Leptin

Recombinant leptin is produced using genetic engineering techniques. The gene encoding leptin is inserted into a host organism, such as Escherichia coli (E. coli), which then produces the leptin protein. This method allows for the large-scale production of leptin for research and therapeutic purposes.

Pegylation

Pegylation refers to the process of attaching polyethylene glycol (PEG) chains to a molecule, in this case, leptin. The addition of PEG increases the molecular size of the protein, which can enhance its stability, solubility, and half-life in the bloodstream. Pegylation can also reduce the immunogenicity of the protein, making it less likely to provoke an immune response.

Pegylated Rat Leptin Recombinant

Pegylated Rat Leptin Recombinant is a single, non-glycosylated polypeptide chain containing 147 amino acids and an additional alanine at the N-terminus. The molecular mass of this pegylated protein is approximately 35.6 kDa, including the 20 kDa PEG moiety .

Biological Activity

The pegylation of leptin does not significantly alter its biological activity. Pegylated leptin retains its ability to bind to leptin receptors and exert its physiological effects. Studies have shown that pegylated leptin can effectively reduce body weight and food intake in animal models . It also plays a role in regulating glucose metabolism and has potential therapeutic applications in treating obesity and metabolic disorders.

Applications and Research

Pegylated Rat Leptin Recombinant is used extensively in research to study the physiological and metabolic effects of leptin. It is also being investigated for its potential therapeutic applications in treating obesity, diabetes, and other metabolic disorders. The enhanced stability and prolonged half-life of pegylated leptin make it a promising candidate for clinical use.

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