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Leptin - triple mutant (L39A/D40A/F41A)

Obesity Factor

rat, recombinant, E. coli

Cat. No. Amount Price (EUR) Buy / Note
PR-487 100 μg 253,00 Add to Basket/Quote Add to Notepad

For in vitro use only!

Shipping: shipped at ambient temperature

Storage Conditions: store at -20 °C
avoid freeze/thaw cycles

Shelf Life: 12 months

Molecular Weight: 16 kDa

Purity: > 95 % (SDS-PAGE)

Form: lyophilised (Leptin is lyophilised from a solution containing 0.003 mM NaHCO3)

Solubility: It is recommended to reconstitute the lyophilised Leptin mutant in sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100 μg/ml, which can then be further diluted to other aqueous solutions. At low concentrations addition of a carrier protein (0.1% HSA or BSA) is suggested.

Activity: This Leptin triple mutant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.

Leptin inhibits food intake and stimulates energy expenditure. Leptin also has thermogenic actions and regulates enzymes of fatty acid oxidation. Severe hereditary obesity in rodents and humans is caused by defects in leptin production. In addition to its critical role in the physiologic regulation of body weight leptin has a variety of other physiologic and pathologic functions resembling those of cytokines. These functions include the regulation of hematopoiesis, angiogenesis, wound healing, inflammation, and immune responses. Recombinant Rat Leptin, one polypeptide chain containing 146 amino acids and additional Ala at the N-terminus and having a molecular mass of {tab??} 16 kDa, was mutated, resulting in a L39A/D40A/F41A mutant. Leptin mutant was purified by proprietary chromatographic techniques.

Amino Acid Sequence: The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln

Selected References:
Theriault et al. (2001) Clinical evaluation of a new non-isotopic leptin immunoassay. Clin. Lab. Sci. 14:6.
Thomas (2004) Leptin and fragility fracture: evidence for a protective effect in humans. Am. J. Med. 117:966.
Schett et al. (2004) Serum leptin level and the risk of nontraumatic fracture. Am. J. Med. 117:952.
Iwamoto et al. (2004) The leptin receptor in human osteoblasts and the direct effect of leptin on bone metabolism. Gynecol. Endocrinol. 19:97.
Mami et al. (2005) Plasma leptin, insulin, and neuropeptide Y concentrations in infants. Arch. Dis. Child. Fetal. Neonatal. Ed. 90:F86.