Leptin - triple mutant (L39A/D40A/F41A)

Obesity Factor

ovine (sheep), recombinant, E. coli

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Leptin - triple mutant (L39A/D40A/F41A) PR-488 100 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: lyophilized (Leptin is lyophilized from a solution containing 0.003 mM NaHCO3)

Solubility: It is recommended to reconstitute the lyophilized Leptin-Antagonist Triple Mutant Ovine recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8, not less than 100μg/ml, which can then be further diluted to other aqueous solutions.

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.

Description:
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 Ovine Leptin, one polypeptide chain containing 146 amino 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-Arg

Selected References:
Laborde et al. (2004) Overexpression of ovine leptin in Pichia pastoris: physiological yeast response to leptin production and characterization of the recombinant hormone. Yeast. 21:249.
Howe et al. (2002) The late gestation increase in circulating ACTH and cortisol in the fetal sheep is suppressed by intracerebroventricular infusion of recombinant ovine leptin. J. Endocrinol. 174:259.
Amstalden et al. (2002) Central infusion of recombinant ovine leptin normalizes plasma insulin and stimulates a novel hypersecretion of luteinizing hormone after short-term fasting in mature beef cows. Biol. Reprod. 66:1555.
Morrison et al. (2002) Effect of intravenous infusion of recombinant ovine leptin on feed intake and serum concentrations of GH, LH, insulin, IGF-1, cortisol, and thyroxine in growing prepubertal ewe lambs. Domest. Anim. Endocrinol. 22:103.
Newby et al. (2001) Effects of recombinant ovine leptin on in vitro lipolysis and lipogenesis in subcutaneous adipose tissue from lactating and nonlactating sheep. J. Anim. Sci. 79:445.
Kauter et al. (2000) Adrenaline, insulin and glucagon do not have acute effects on plasma leptin levels in sheep: development and characterisation of an ovine leptin ELISA. J. Endocrinol. 166:127.