Leptin Mouse, PEG

Pegylated Mouse Leptin Recombinant

Leptin Mono-Pegylated Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and an additional Ala at N-terminus. Pegylated Mouse Leptin contains PEG 20 kDa at its N-terminus and having a molecular mass of 35.6 kDa as determined by mass spectrometry.
Since its enlarged hydrodymanic volume Pegylated Leptin runs on SDS-PAGE as A 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein.
Pegylated Mouse Leptin half-life in circulation after SC injection was over 20 hours. Mouse Leptin was purified by proprietary chromatographic techniques according to Salomon et al (2006) Protein Expression and Purification 47, 128–136 and then pegylated.
Shipped with Ice Packs
Cat. No.
BT20961
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Leptin Ovine

Leptin Ovine Recombinant

Leptin Ovine 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.
Shipped with Ice Packs
Cat. No.
BT21043
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Leptin Ovine, MTS

Leptin Ovine Recombinant, MTS tag

Leptin Ovine MTS tagged Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17.5 kDa.
The Leptin is purified by proprietary chromatographic techniques. The membrane translocating sequence Tag is composed of 10 amino acids Val-Leu-Leu-Pro-Val-Leu-Leu-Ala-Ala-Pro located at the N-terminus.
Shipped with Ice Packs
Cat. No.
BT21116
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Leptin Porcine

Leptin Porcine Recombinant

Leptin Porcine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and additional Ala at N-terminus, having a molecular mass of 16kDa.
The Leptin is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21202
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Leptin Protein

Leptin Human Recombinant

Leptin Human 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.
Shipped with Ice Packs
Cat. No.
BT21273
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Leptin Pufferfish

Leptin Pufferfish Recombinant

Leptin Pufferfish (Takifugu rubripes) Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 16 kDa.
Bioactive Leptin Pufferfish (Takifugu rubripes) Recombinant was prepared according to the sequence published by Kurokawa et al. (2005)Peptides 26, 745-750 in two forms: monomer and covalent dimer. MS analysis revealed molecular masses of 15,291 and 30,585 Da, close to the theoretical values of 15,270 and 30,540 Da. CD spectra revealed high similarity to mammalian leptins. Other details of its preparation will be soon published by Yacobovitz et al (in press), General and Comparative Endocrinology.
The Pufferfish Leptin is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21379
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Leptin qA Human

Leptin Antagonist Quadruple Mutant Human Recombinant

Leptin Quadruple Mutant Human Recombinant is a single polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a Mw of 16 kDa, Human Leptin was mutated, resulting in L39A/D40A/F41A/I42A.
Leptin Antagonist Quadruple Mutant was purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21465
Source
Escherichia coli.
Appearance
White lyophilized (freeze-dried) powder.

Leptin qA Ovine

Leptin Antagonist Quadruple Mutant Ovine Recombinant

Leptin Antagonist Quadruple Mutant Ovine 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, Leptin was mutated, resulting in L39A/D40A/F41A/I42A mutant.
Leptin Antagonist Quadruple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21565
Source
Escherichia coli.
Appearance
White lyophilized (freeze-dried) powder.

Leptin Rabbit

Leptin Rabbit Recombinant

Leptin Rabbit 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.
Shipped with Ice Packs
Cat. No.
BT21653
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Leptin Rat

Leptin Rat Recombinant

Leptin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 147 amino acids and having a molecular mass of 16 kDa.
The Leptin is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21749
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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 .

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