Leptin Pufferfish
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.
Description
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.
Product Specs
ALPGALDAMDVEKMKSKVTWKAQGLVARIDKHFPDRGLRFDTDKVE
GSTSVVASLESYNNLISDRFGGVSQIKTEISSLAGYLNHWREGNCQE
QQPKVWPRRNIFNHTVSLEALMRVREFLKLLQKNVDLLERC
Product Science Overview
Leptin is a peptide hormone primarily produced by adipose tissue in mammals. It plays a crucial role in regulating energy balance by inhibiting hunger, which in turn diminishes fat storage in adipocytes. The hormone communicates the status of energy reserves to the brain, particularly the hypothalamus, thereby influencing appetite and metabolic rate .
The leptin gene was first identified in mammals in 1994 by Jeffrey Friedman and his team. Since then, leptin genes have been discovered across various vertebrate species, including fish, amphibians, reptiles, and birds . The leptin protein structure has been conserved throughout evolution, although there are significant differences in the primary amino acid sequences among different species .
The pufferfish (Takifugu rubripes) leptin gene was identified and cloned to study its structure and function. The recombinant leptin from pufferfish is produced in Escherichia coli as a single, non-glycosylated polypeptide chain with a molecular mass of approximately 16 kDa . This recombinant leptin is bioactive and has been used in various studies to understand leptin’s role in fish physiology.
The preparation of recombinant leptin involves cloning the leptin gene from pufferfish into a suitable expression vector, which is then introduced into Escherichia coli. The bacteria are cultured, and the leptin protein is expressed, harvested, and purified. The resulting product is a sterile, filtered, white lyophilized (freeze-dried) powder .
Recombinant leptin from pufferfish has been instrumental in studying the hormone’s role in non-mammalian species. It has provided insights into the evolutionary conservation and divergence of leptin’s function across different vertebrate classes. Additionally, understanding leptin’s role in fish can have applications in aquaculture, where managing energy reserves is crucial for the growth and health of commercially important species .
