Leptin tA Ovine

Leptin Antagonist Triple Mutant Ovine Recombinant

Leptin Antagonist Triple 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 mutant. Leptin Antagonist Triple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20045
Source
Escherichia coli.
Appearance
White lyophilized (freeze-dried) powder.

Leptin Bovine

Leptin Bovine Recombinant

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.
Shipped with Ice Packs
Cat. No.
BT20160
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Leptin Chicken

Leptin Chicken Recombinant

Leptin Chicken Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 145 amino acids and having a molecular mass of 16 kDa.
The Leptin is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20266
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Leptin Dog

Leptin Dog Recombinant

Leptin Dog 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.
BT20363
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Leptin Horse

Leptin Horse Recombinant

Leptin Horse 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.
BT20447
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Leptin Human

Human Leptin

Leptin Human produced syntheticaly contains 35 amino acids (22-56 a.a.) having a molecular mass of 3950.6 Dalton.
Shipped with Ice Packs
Cat. No.
BT20546
Source
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Leptin Human, His

Leptin Human Recombinant, His Tag

Leptin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing amino acids 48-167 and having a total molecular mass of 19 kDa including the 4 kDa His tag.
The Leptin is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20632
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Leptin Human, N82K

Leptin Human Recombinant, N82K

Leptin N82K Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids (and additional Ala at N-terminus acids) and having a molecular mass of 16kDa.

The Leptin N82K is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT20695
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Leptin Human, N82K PEG

Leptin N82K Human Recombinant, Pegylated

Pegylated Leptin N82K Human Recombinant produced in E.Coli is  a single non-glycosilated polypeptide chain containing 146 amino acids, an additional Ala at N-terminus and one molecule of PEG 20 kDa at its N-terminus acids and having a molecular weight of 35.6kDa. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. Pegylated Leptin N82K Human Recombinant was purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT20775
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Leptin Mouse

Leptin Mouse Recombinant

Leptin Mouse 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.
BT20872
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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