Leptin Bovine

Leptin Bovine Recombinant
Cat. No.
BT20160
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.
Shipped with Ice Packs
In Stock

Description

Leptin Bovine 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.

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 signaling the body's energy stores to the brain.
Description
Recombinant Bovine Leptin, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 146 amino acids with a molecular weight of 16 kDa. The purification process involves proprietary chromatographic techniques.
Physical Appearance
Sterile white powder obtained by lyophilization (freeze-drying).
Formulation
The protein was lyophilized from a 1 mg/mL solution containing 0.02% NaHCO3.
Solubility
To reconstitute the lyophilized Leptin, it is recommended to dissolve it in sterile 0.4% NaHCO3 at a concentration of at least 100 µg/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 should be stored desiccated below -18°C. After reconstitution, the Leptin solution can be stored at 4°C for 2-7 days. For extended storage, freezing below -18°C is recommended. To enhance stability during long-term storage, adding a carrier protein (0.1% HSA or BSA) is advisable. 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
Protein quantification was performed using UV spectroscopy at 280 nm. An extinction coefficient of 0.2 was used for a 0.1% (1 mg/mL) solution, a value determined by the PC GENE computer analysis program (IntelliGenetics) based on the protein's amino acid sequence.
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

Discovery and Function

Leptin was first discovered in 1994 by Jeffrey Friedman and his colleagues at Rockefeller University. The hormone is encoded by the ob gene and is involved in various physiological processes, including:

  • Regulation of appetite: Leptin acts on the hypothalamus in the brain to inhibit appetite and increase energy expenditure.
  • Energy balance: It helps maintain energy homeostasis by signaling the brain about the body’s energy status.
  • Endocrine functions: Leptin is involved in the regulation of immune and inflammatory responses, hematopoiesis (formation of blood cells), angiogenesis (formation of new blood vessels), and wound healing .
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 Escherichia coli (E. coli), to produce the hormone in large quantities. Recombinant leptin is used in research and therapeutic applications to study its effects and potential treatments for conditions like obesity and metabolic disorders .

Bovine Recombinant Leptin

Bovine recombinant leptin (rbLeptin) is leptin derived from cattle. It is used in various research studies to understand its role in energy balance and body weight regulation in bovine species. Bovine leptin has similar functions to human leptin, including:

  • Regulation of food intake: Bovine leptin helps regulate appetite and energy expenditure in cattle.
  • Energy homeostasis: It plays a role in maintaining energy balance by signaling the brain about the body’s energy status.
  • Reproductive functions: Leptin is also involved in reproductive processes, influencing fertility and pregnancy .
Applications and Research

Recombinant bovine leptin is used in various research studies to explore its potential applications in agriculture and medicine. Some key areas of research include:

  • Obesity and metabolic disorders: Studying the effects of leptin on obesity and related metabolic disorders to develop potential treatments.
  • Reproductive health: Investigating the role of leptin in reproductive processes and its impact on fertility and pregnancy.
  • Energy balance in livestock: Understanding how leptin regulates energy balance in cattle to improve livestock management and productivity .

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