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Growth Factors

Leptin

CSF

Prolactin PRL

RANK Ligand

Retinol Binding Protein

Stem Cell Factor

CTGF

Transforming Growth Factor

EGF

Epigen

Erythropoietin

VEGF Protein

Fibroblast Growth Factor

Other Growth Factors

Galectin

Growth Hormone

HDGF

Hepatocyte Growth Factor

IGFBP

Insulin-Like Growth Factor

Insulin

Keratinocyte Growth Factor

Macrophage Migration Inhibitory Factor

Melanoma Inhibitory Activity

Myostatin

Noggin

NOV

Omentin

Oncostatin-M

Osteopontin

Osteoprotegerin

PDGF

Periostin

Placental Growth Factor

Placental Lactogen

Product List

Leptin Rat, PEG

Pegylated Rat Leptin Recombinant

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.

Shipped with Ice Packs

Cat. No.

BT21819

Source

Escherichia Coli.

Appearance

Sterile Filtered White lyophilized powder.

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Leptin Receptor Chicken

Leptin Receptor Chicken Recombinant

Leptin Binding Domain Chicken Recombinant, also known as Leptin Receptor, is produced in E. coli. This non-glycosylated polypeptide chain comprises 208 amino acids, resulting in a molecular weight of 24.5 kDa. It encompasses the cytokine binding domain of the chicken leptin receptor, specifically amino acids 420-626. Purification of the Leptin Binding Domain is achieved through proprietary chromatographic methods.

Shipped with Ice Packs

Cat. No.

BT21884

Source

Escherichia Coli.

Appearance

A clear, sterile solution without any color, with a concentration of 0.4 mg/ml.

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Leptin Salamander

Leptin Salamander Recombinant

Recombinant Salamander Leptin, expressed in E. coli, is a non-glycosylated polypeptide chain consisting of 146 amino acids and an additional alanine residue at the N-terminus. With a molecular weight of 16 kDa, it is purified using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT21967

Source

Escherichia Coli.

Appearance

Sterile, white, lyophilized (freeze-dried) powder.

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Leptin tA Human

Leptin Antagonist Triple Mutant Human Recombinant

Leptin Antagonist Triple Mutant Human Recombinant is a single, non-glycosylated polypeptide chain consisting of 146 amino acids and an additional alanine residue at the N-terminus. With a molecular weight of 16 kDa, this variant features three mutations (L39A/D40A/F41A). Purification is achieved through proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT22030

Source

Escherichia coli.

Appearance

White, lyophilized powder.

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Leptin tA Human, PEG

Leptin Antagonist Triple Mutant Human Recombinant, Pegylated

Pegylated Leptin Antagonist Triple Mutant Human Recombinant is a single, non-glycosylated polypeptide chain composed of 146 amino acids, with an additional alanine residue at the N-terminus. It has a molecular weight of 35.6 kDa. The Leptin sequence was mutated, resulting in the substitutions L39A/D40A/F41A. Due to its enlarged hydrodynamic volume, it appears as a 48 kDa protein on SDS-PAGE and elutes as an over 200 kDa protein in gel-filtration using Superdex 200. The Leptin Antagonist Triple Mutant Human Recombinant is mono-pegylated with a 20 kDa PEG molecule and was purified using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT22228

Source

Escherichia coli.

Appearance

White, lyophilized powder.

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Leptin tA Mouse

Leptin Antagonist Triple Mutant Mouse Recombinant

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.

Shipped with Ice Packs

Cat. No.

BT22301

Source

Escherichia coli.

Appearance

White, lyophilized powder.

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Leptin tA Mouse, PEG

Leptin Antagonist Triple Mutant Pegylated Mouse Recombinant

Leptin Antagonist Triple Mutant Mouse Recombinant is a single, non-glycosylated polypeptide chain consisting of 146 amino acids with an additional Alanine residue at the N-terminus. It has a molecular weight of approximately 16 kDa.
This modified Mouse Leptin antagonist features the mutations L39A/D40A/F41A.
The molecule is conjugated to a 20 kDa mono-PEG molecule at the N-terminus, resulting in a total weight of 35.6 kDa. However, it appears as a 48 kDa band on gel electrophoresis.
The purification of Leptin Antagonist Triple Mutant Mouse Recombinant was achieved using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT22373

Source

Escherichia coli.

Appearance

The product appears as a white, lyophilized (freeze-dried) powder.

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Leptin tA Ovine, PEG

Leptin Antagonist Triple Mutant Ovine Recombinant, Pegylated

Pegylated Leptin Antagonist Triple Mutant Ovine Recombinant is a single, non-glycosylated polypeptide chain containing 146 amino acids and an additional Alanine at the N-terminus. It has a molecular mass of approximately 35.6 kDa. The Leptin was mutated, resulting in the L39A/D40A/F41A mutant. Due to its enlarged hydrodynamic volume, it runs on SDS-PAGE as a 48 kDa protein and in gel-filtration on Superdex 200 as an over 200 kDa protein. The Leptin Antagonist Triple Mutant Ovine Recombinant is mono-pegylated with 20 kDa PEG and was purified by proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT22570

Source

Escherichia coli.

Appearance

White, lyophilized (freeze-dried) powder.

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Leptin tA Rat

Leptin Antagonist Triple Mutant Rat Recombinant

Leptin Antagonist Triple Mutant Rat Recombinant 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 leptin protein was mutated, resulting in the L39A/D40A/F41A mutant. This recombinant protein was purified using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT22681

Source

Escherichia coli.

Appearance

White, lyophilized powder.

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Leptin tA Rat, PEG

Leptin Antagonist Triple Mutant Pegylated Rat Recombinant

Leptin Antagonist Triple Mutant Rat Recombinant is a single, non-glycosylated polypeptide chain containing 146 amino acids with an additional Alanine at the N-terminus. It has a molecular mass of approximately 16 kDa. This recombinant protein is a mutated form of Rat Leptin antagonist, featuring the mutations L39A/D40A/F41A. A 20 kDa mono-PEG molecule is attached to the N-terminus, resulting in a total molecular weight of 35.6 kDa. During SDS-PAGE analysis, the Rat Leptin triple antagonist appears as a 48 kDa band. The protein is purified using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT22757

Source

Escherichia coli.

Appearance

White, lyophilized powder.

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Introduction

Definition and Classification

Leptin is a hormone predominantly produced by adipocytes (fat cells) and plays a crucial role in regulating energy balance by inhibiting hunger. It is classified as a protein hormone and is encoded by the LEP gene.

Biological Properties

Key Biological Properties: Leptin is a 16-kDa circulating hormone that acts as a major regulator for food intake and energy homeostasis.

Expression Patterns: Leptin is primarily expressed in white adipose tissue but is also produced in smaller amounts by other tissues such as the stomach, placenta, and mammary gland.

Tissue Distribution: Leptin receptors are widely distributed in the brain, particularly in the hypothalamus, as well as in peripheral tissues including the liver, skeletal muscle, and immune cells .

Biological Functions

Primary Biological Functions: Leptin’s main function is to regulate long-term energy balance by inhibiting hunger and controlling energy expenditure. It also plays a role in metabolism, endocrine system regulation, and immune system function.

Role in Immune Responses and Pathogen Recognition: Leptin influences immune responses by modulating the activity of immune cells, including T cells and macrophages. It has been shown to enhance the body’s ability to recognize and respond to pathogens.

Modes of Action

Mechanisms with Other Molecules and Cells: Leptin acts via its receptor, LepRb, on specialized neuronal populations in the brain, mainly in the hypothalamus and brainstem.

Binding Partners: Leptin binds to its receptor LepRb, which is expressed by various cell types in the brain and peripheral tissues.

Downstream Signaling Cascades: Upon binding to its receptor, leptin activates several downstream signaling pathways, including the JAK/STAT pathway, MAP kinase, and PI-3 kinase pathways.

Regulatory Mechanisms

Control of Expression and Activity: Leptin expression and protein levels are regulated by multiple factors, including hormones such as insulin, glucocorticoids, and catecholamines .

Transcriptional Regulation: The transcription of the LEP gene is influenced by various metabolic and hormonal signals.

Post-Translational Modifications: Leptin undergoes post-translational modifications that affect its stability and activity.

Applications

Biomedical Research: Leptin is extensively studied in the context of obesity, diabetes, and metabolic disorders.

Diagnostic Tools: Leptin levels can be measured to assess metabolic health and diagnose conditions such as leptin deficiency.

Therapeutic Strategies: Leptin replacement therapy is used to treat conditions like congenital leptin deficiency and lipodystrophy.

Role in the Life Cycle

Development to Aging and Disease: Leptin plays a critical role throughout the life cycle, from fetal development to aging. It influences growth, reproductive function, and immune responses. Dysregulation of leptin levels is associated with various diseases, including obesity, diabetes, and neurodegenerative disorders.