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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 Mouse, PEG

Pegylated Mouse Leptin Recombinant

This product consists of mono-pegylated recombinant mouse leptin. Produced in E. coli, it is a single, non-glycosylated polypeptide chain of 146 amino acids with an additional alanine at the N-terminus. The PEGylation, achieved with a 20 kDa PEG molecule at the N-terminus, results in a 35.6 kDa protein as determined by mass spectrometry. Notably, the pegylation affects its apparent size in SDS-PAGE (48 kDa) and gel filtration (over 100 kDa) due to its increased hydrodynamic volume. This modification extends the protein's half-life in circulation to over 20 hours following subcutaneous injection. The purification process involves proprietary chromatographic methods as outlined in Salomon et al. (2006) Protein Expression and Purification 47, 128–136, followed by the pegylation step.

Shipped with Ice Packs

Cat. No.

BT20961

Source

Escherichia Coli.

Appearance

The product appears as a white, lyophilized powder that has undergone sterile filtration.

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Leptin Ovine

Leptin Ovine Recombinant

Recombinant Ovine Leptin, expressed in E. coli, is a single-chain polypeptide consisting of 146 amino acids. This non-glycosylated protein has a molecular weight of 16 kDa and is purified using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT21043

Source

Escherichia Coli.

Appearance

White, lyophilized (freeze-dried) powder, sterile filtered.

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Leptin Ovine, MTS

Leptin Ovine Recombinant, MTS tag

Recombinant Ovine Leptin, tagged with an MTS sequence, is produced in E. coli. This non-glycosylated polypeptide chain consists of 157 amino acids, resulting in a molecular weight of 17.5 kDa. Purification is achieved using proprietary chromatographic techniques. The N-terminal MTS tag, responsible for membrane translocation, comprises a 10 amino acid sequence: Val-Leu-Leu-Pro-Val-Leu-Leu-Ala-Ala-Pro.

Shipped with Ice Packs

Cat. No.

BT21116

Source

Escherichia Coli.

Appearance

Sterile white powder obtained by lyophilization (freeze-drying).

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Leptin Porcine

Leptin Porcine Recombinant

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

Shipped with Ice Packs

Cat. No.

BT21202

Source

Escherichia Coli.

Appearance

Sterile white powder obtained by lyophilization (freeze-drying).

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Leptin Protein

Leptin Human Recombinant

Recombinant Human Leptin, produced in E. coli, is a single polypeptide chain without glycosylation. It consists of 146 amino acids, resulting in a molecular weight of 16 kDa. The purification process involves proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT21273

Source

Escherichia Coli.

Appearance

White, lyophilized (freeze-dried) powder, sterile-filtered.

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Leptin Pufferfish

Leptin Pufferfish Recombinant

Recombinant Leptin from the Pufferfish (Takifugu rubripes) is produced in E. coli and purified to a single, non-glycosylated polypeptide chain with a molecular weight of 16 kDa. This product is offered in both monomeric and covalently linked dimeric forms. Mass spectrometry analysis confirms the expected molecular masses of approximately 15.3 kDa and 30.6 kDa for the monomer and dimer, respectively. Circular dichroism spectroscopy demonstrates a high degree of structural similarity to mammalian leptins. Detailed characterization and production methods will be available in an upcoming publication by Yacobovitz et al. in General and Comparative Endocrinology. The purification process employs proprietary chromatographic techniques to ensure high purity.

Shipped with Ice Packs

Cat. No.

BT21379

Source

Escherichia Coli.

Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

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Leptin qA Human

Leptin Antagonist Quadruple Mutant Human Recombinant

Recombinant Human Leptin Quadruple Mutant is a single polypeptide chain with a molecular weight of 16 kDa. It consists of 146 amino acids and an additional alanine residue at the N-terminus. This mutant form of human leptin contains the following mutations: L39A/D40A/F41A/I42A. The purification process involves proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT21465

Source

Escherichia coli.

Appearance

White, lyophilized powder.

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Leptin qA Ovine

Leptin Antagonist Quadruple Mutant Ovine Recombinant

Leptin Antagonist Quadruple Mutant Ovine 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. The Leptin protein was mutated, resulting in the L39A/D40A/F41A/I42A mutant. Leptin Antagonist Quadruple Mutant Ovine Recombinant was purified using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT21565

Source

Escherichia coli.

Appearance

White, lyophilized powder.

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Leptin Rabbit

Leptin Rabbit Recombinant

Leptin Rabbit Recombinant is a non-glycosylated polypeptide chain comprising 146 amino acids, with a molecular weight of 16 kDa. It is produced in E. coli and purified using proprietary chromatographic techniques to ensure high purity.

Shipped with Ice Packs

Cat. No.

BT21653

Source

Escherichia Coli.

Appearance

White, lyophilized (freeze-dried) powder, sterile filtered for purity.

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Leptin Rat

Leptin Rat Recombinant

Leptin Rat Recombinant, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 16 kDa, comprising 147 amino acids. It undergoes purification using proprietary chromatographic methods.

Shipped with Ice Packs

Cat. No.

BT21749

Source

Escherichia Coli.

Appearance

White, lyophilized (freeze-dried) powder, sterile filtered.

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Showing 11 to 20 of 30 results

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.