Leptin tA Mouse

Leptin Antagonist Triple Mutant Mouse Recombinant
Cat. No.
BT22301
Source
Escherichia coli.
Synonyms
Appearance
White lyophilized (freeze-dried) powder.
Purity
Greater than 99.0% 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.
Shipped with Ice Packs
In Stock

Description

Leptin Antagonist Triple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, LEP was mutated, resulting in L39A/D40A/F41A mutant. Leptin Antagonist Triple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.

Product Specs

Description
Recombinant Leptin Antagonist Triple Mutant Mouse is a single, non-glycosylated polypeptide chain. It contains 146 amino acids, with an additional alanine at the N-terminus, and has a molecular mass of approximately 16 kDa. The protein was mutated, resulting in the L39A/D40A/F41A mutant. Purification was achieved using proprietary chromatographic techniques.
Physical Appearance
White, lyophilized powder.
Formulation
The protein was lyophilized from a concentrated solution (0.65 mg/ml) containing 0.003 mM NaHCO3.
Solubility
Reconstitute the lyophilized Leptin Antagonist Triple Mutant Mouse in sterile water or sterile 0.4% NaHCO3 adjusted to a pH of 8-9. The final concentration should be at least 100 µg/ml. This solution can be further diluted with other aqueous solutions.
Stability
Lyophilized Leptin Antagonist Triple Mutant Mouse remains stable at room temperature for several weeks. However, for long-term storage, it should be stored desiccated below -18°C. Once reconstituted at a concentration greater than 0.1 mg/ml and up to 2 mM, and after filter sterilization, it can be stored at 4°C or room temperature for several weeks. This makes it suitable for long-term infusion studies using osmotic pumps. At lower concentrations, adding a carrier protein (0.1% HSA or BSA) is recommended. Avoid freeze-thaw cycles.
Purity
Purity exceeds 99.0%, as determined by: (a) Gel filtration analysis. (b) SDS-PAGE analysis.
Biological Activity
THE BioTek's Leptin Antagonist Triple Mutant Mouse effectively inhibits Leptin-induced proliferation of BAF/3 cells stably transfected with the long form of the human Leptin receptor. It also inhibits various Leptin effects in several in vitro bioassays.
Protein Content
Protein quantification was performed using UV spectroscopy at 280 nm. An absorbency value of 0.21 was used as the extinction coefficient for a 0.1% (1 mg/ml) solution at pH 8.0. This value was calculated using the PC GENE computer analysis program of protein sequences (IntelliGenetics).
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-Gln.

Product Science Overview

Introduction

Leptin is a hormone predominantly made by adipose cells and enterocytes in the small intestine that helps to regulate energy balance by inhibiting hunger. It is often referred to as the “satiety hormone” or “fat hormone.” Leptin plays a crucial role in body weight regulation and metabolism.

Leptin Antagonist Triple Mutant

The Leptin Antagonist Triple Mutant (Mouse Recombinant) is a modified form of the leptin protein. This recombinant protein is designed to inhibit the action of leptin, making it a valuable tool for studying leptin’s role in various physiological processes.

Structure and Composition

The Leptin Antagonist Triple Mutant is a single non-glycosylated polypeptide chain containing 146 amino acids, with an additional alanine at the N-terminus. The molecular weight of this protein is approximately 16 kDa . The antagonist is created by introducing three specific mutations in the leptin protein: L39A, D40A, and F41A . These mutations significantly reduce the binding affinity of leptin to its receptor, thereby inhibiting its biological activity.

PEGylation

To enhance the stability and solubility of the Leptin Antagonist Triple Mutant, it is often PEGylated. PEGylation involves the attachment of polyethylene glycol (PEG) molecules to the protein. In this case, a 20 kDa mono-PEG is attached to the N-terminus of the protein, resulting in a combined molecular weight of approximately 35.6 kDa . The PEGylated form runs as a 48 kDa protein on SDS-PAGE due to the added mass of the PEG molecule .

Production and Purification

The Leptin Antagonist Triple Mutant is produced using recombinant DNA technology in Escherichia coli (E. coli) cells . The protein is then purified using proprietary chromatographic techniques to achieve a purity greater than 99.0%, as determined by gel filtration analysis and SDS-PAGE .

Applications

The Leptin Antagonist Triple Mutant is used in various research applications to study the role of leptin in metabolism, obesity, and related disorders. It is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of the human leptin receptor . Additionally, it inhibits various leptin effects in several in vitro bioassays .

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