Source:

Escherichia coli.

Molecular Weight:

16.3 kDa, observed by reducing SDS-PAGE.

Purity:

> 95% as analyzed by SDS-PAGE and HPLC.

Biological activity:

ED50 < 10 µg/mL, measured by a cell proliferation assay using LoVo cells, corresponding to a specific activity of > 100 units/mg.

AA Sequence:

MVPIHKVQD DTKTLIKTIV TRINDISHTQ SVSARQRVTG LDFIPGLHPI LSLSKMDQTL AVYQQILTSL PSQNVLQIAH DLENLRDLLH LLAFSKSCSL PQTRGLQKPE SLDGVLEASL YSTEVVALSR LQGSLQDILQ QLDLSPEC

Endotoxin:

< 0.2 EU/μg, determined by LAL method.

Formulation:

Lyophilized after extensive dialysis against 50 mM Tris, pH8.0.

Background:

Leptin is a cytokine belonging to the Interleukin 6 family, and has a four-helix bundle structure. Leptin is encoded by the ob gene, and produced and secreted by white adipose tissue. The receptors of Leptin are Type I cytokine receptors, which exist in two different forms: a short form expressed in multiple tissues, and a long form expressed exclusively in the central nervous system (CNS). Upon binding to Leptin, the receptors activate the JAK/STAT3 pathway and PI3K, and stimulate transcriptional programs that regulate feeding behavior, metabolic rate, endocrine axes, and glucose fluxes. The deficiency of Leptin in human and mouse causes morbid obesity, diabetes, and neuroendocrine anomalies. Leptin also has effects on reproduction and immunity. In summary, Leptin is a pivotal cytokine controlling energy balance, and as such has profound effects on human health. Recombinant rat Leptin (rrLeptin) produced in E.coli is a single non-glycosylated polypeptide chain containing 147 amino acids. A fully biologically active molecule, rrLeptin has a molecular mass of 16.3 kDa analyzed by reducing SDS-PAGE and is obtained by proprietary chromatographic techniques at GenScript.

Usage:

This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. For research use only.

Physical Appearance:

Sterile Filtered White lyophilized (freeze-dried) powder.

Reconstitution:

Reconstituted in ddH2O at 100 μg/mL.

Storage:

Lyophilized recombinant rat Leptin (rrLeptin) remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, rrLeptin remains stable up to 2 weeks at 4°C or up to 3 months at -20°C.