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Manufactured by BioVendor

Leptin Rabbit E. coli

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:E. coli
  • Other names:Obesity factor, Obese protein, LEP, OB, OBS
  • Species:Rabbit
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Cat. No. Size Price


RP1765070100 100 μg
RP1765070200 200 µg
RP1765071000 1 mg
PubMed Product Details
Technical Data

Type

Recombinant protein

Description

Leptin Rabbit 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.

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.

Source

E. coli

Purity

Greater than 95.0% as determined by(a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.

Biological Activity

Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

Formulation

The protein was lyophilized from a concentrated (1 mg/ml) solution with 0.0045 mM NaHCO3.

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below –18°C. Upon reconstitution Leptin should be stored at 4°C between 2–7 days and for future use below –18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

Physical Appearance

Sterile filtered white lyophilized (freeze-dried) powder.

Summary

Research topic

Diabetology - Other Relevant Products, Energy metabolism and body weight regulation, Reproduction

Summary

Leptin, the product of the ob (obese) gene, is a single-chain 16 kDa proteohormone consisting of 146 amino acid residues. Leptin is produced by differentiated adiocytes, although production have been demonstrated in other tissues, such as fundus of the stomach, the sceletal muscle, the liver, and the placenta. Leptin is considered to play an important role in appetite control, fat metabolism and body weight regulation. It targets the central nervous system, in particular the hypothalamus, suppressing food intake and stimulating energy expenditure. In humans, leptin levels correlate with body mass index (BMI) and percentage body fat, and are elevated even in obese individuals. Leptin has a dual action; it decreases the appetite and increases energy consumption, causing more fat to be burned.

Summary References (20)

References to Leptin

  • Auwerx J, Staels B. Leptin (Review article). The Lancet . 13, 737 (1998);
  • Blum WF, Englaro P, Hanitsch S, Juul A, Hertel NT, Muller J, Skakkebaek NE, Heiman ML, Birkett M, Attanasio AM, Kiess W, Rascher W. Plasma leptin levels in healthy children and adolescents: dependence on body mass index, body fat mass, gender, pubertal stage, and testosterone. J Clin Endocrinol Metab. 1997 Sep;82 (9):2904-10
  • Chehab FF, Mounzih K, Lu R, Lim ME. Early onset of reproductive function in normal female mice treated with leptin. Science. 1997 Jan 3;275 (5296):88-90
  • Clement K, Vaisse C, Lahlou N, Cabrol S, Pelloux V, Cassuto D, Gourmelen M, Dina C, Chambaz J, Lacorte JM, Basdevant A, Bougneres P, Lebouc Y, Froguel P, Guy-Grand B. A mutation in the human leptin receptor gene causes obesity and pituitary dysfunction. Nature. 1998 Mar 26;392 (6674):398-401
  • Cohen B, Novick D, Rubinstein M. Modulation of insulin activities by leptin. Science. 1996 Nov 15;274 (5290):1185-8
  • Considine RV, Sinha MK, Heiman ML, Kriauciunas A, Stephens TW, Nyce MR, Ohannesian JP, Marco CC, McKee LJ, Bauer TL, et al. Serum immunoreactive-leptin concentrations in normal-weight and obese humans. N Engl J Med. 1996 Feb 1;334 (5):292-5
  • Friedman JM, Halaas JL. Leptin and the regulation of body weight in mammals. Nature. 1998 Oct 22;395 (6704):763-70
  • Halaas JL, Gajiwala KS, Maffei M, Cohen SL, Chait BT, Rabinowitz D, Lallone RL, Burley SK, Friedman JM. Weight-reducing effects of the plasma protein encoded by the obese gene. Science. 1995 Jul 28;269 (5223):543-6
  • Harigaya A, Nagashima K, Nako Y, Morikawa A. Relationship between concentration of serum leptin and fetal growth. J Clin Endocrinol Metab. 1997 Oct;82 (10):3281-4
  • Lonnqvist F, Arner P, Nordfors L, Schalling M. Overexpression of the obese (ob) gene in adipose tissue of human obese subjects. Nat Med. 1995 Sep;1 (9):950-3
  • Maffei M, Halaas J, Ravussin E, Pratley RE, Lee GH, Zhang Y, Fei H, Kim S, Lallone R, Ranganathan S, et al. Leptin levels in human and rodent: measurement of plasma leptin and ob RNA in obese and weight-reduced subjects. Nat Med. 1995 Nov;1 (11):1155-61
  • Montague CT, Farooqi IS, Whitehead JP, Soos MA, Rau H, Wareham NJ, Sewter CP, Digby JE, Mohammed SN, Hurst JA, Cheetham CH, Earley AR, Barnett AH, Prins JB, O'Rahilly S. Congenital leptin deficiency is associated with severe early-onset obesity in humans. Nature. 1997 Jun 26;387 (6636):903-8
  • Pelleymounter MA, Cullen MJ, Baker MB, Hecht R, Winters D, Boone T, Collins F. Effects of the obese gene product on body weight regulation in ob/ob mice. Science. 1995 Jul 28;269 (5223):540-3
  • Ricci MR, Lee MJ, Russell CD, Wang Y, Sullivan S, Schneider SH, Brolin RE, Fried SK. Isoproterenol decreases leptin release from rat and human adipose tissue through posttranscriptional mechanisms. Am J Physiol Endocrinol Metab. 2005 Apr;288 (4):E798-804
  • Schubring C, Prohaska F, Prohaska A, Englaro P, Blum W, Siebler T, Kratzsch J, Kiess W. Leptin concentrations in maternal serum and amniotic fluid during the second trimenon: differential relation to fetal gender and maternal morphometry. Eur J Obstet Gynecol Reprod Bi. 1999 Oct;86 (2):151-7
  • Spiegelman BM, Flier JS. Adipogenesis and obesity: rounding out the big picture. Cell. 1996 Nov 1;87 (3):377-89
  • Tartaglia LA. The leptin receptor. J Biol Chem. 1997 Mar 7;272 (10):6093-6
  • Tritos NA, Mantzoros CS. Leptin: its role in obesity and beyond. Diabetologia. 1997 Dec;40 (12):1371-9
  • Zhang F, Basinski MB, Beals JM, Briggs SL, Churgay LM, Clawson DK, DiMarchi RD, Furman TC, Hale JE, Hsiung HM, Schoner BE, Smith DP, Zhang XY, Wery JP, Schevitz RW. Crystal structure of the obese protein leptin-E100. Nature. 1997 May 8;387 (6629):206-9
  • Zhang Y, Proenca R, Maffei M, Barone M, Leopold L, Friedman JM. Positional cloning of the mouse obese gene and its human homologue. Nature. 1994 Dec 1;372 (6505):425-32
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