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Manufactured by BioVendor

Leptin Mouse E. coli Tag free

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


RD272001100 0.1 mg
PubMed Product Details
Technical Data

Type

Recombinant protein

Description

UniProtKB acc.no. P41160

Amino Acid Sequence

MVPIQKVQDDTKTLIKTIVTRINDISHTQSVSAKQRVTGLDFIPGLHPILSLSKMDQTLAVYQQVLTSLPSQNVLQIANDLENLRDLLHLLAFSKSCSLPQTSGLQKPESLDGVLEASLYSTEVVALSRLQGSLQDILQQLDVSPEC

Source

E. coli

Purity

>98% by SDS PAGE gel analysis

SDS-PAGE Gel

14% SDS-PAGE separation of Mouse Leptin
1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa
2. reduced and heated sample, 5μg/lane
3. non-reduced and non-heated sample, 5μg/lane

Biological Activity

Biological activity of Mouse Leptin is performed in two different mouse obesity models, ob/ob and NZO. Both strains of mice were treated via intraperitoneal injection once daily at a dose of 5 µg Leptin/gm of body weight for 7 days. Significant effects on body weight, food consumption, and plasma glucose levels were observed to saline-treated controls.

Endotoxin

< 1.0 EU/ug

Formulation

Filtered (0.4 μm) and lyophilized with 0.1% TFA.

Reconstitution

Add injection water to prepare a working stock solution of 1.0 mg/mL and let the lyophilized pellet dissolve completely. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store at –80°C. Filter sterilize your culture media/working solutions containing this non-sterile product before using in cell culture.

Applications

Western blotting, ELISA

Shipping

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

Storage/Expiration

Store the lyophilized protein at –80 °C. Lyophilized protein remains stable until the expiry date when stored at –80 °C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80 °C for long term storage. Reconstituted protein can be stored at 4 °C for a week.

Quality Control Test

BCA to determine quantity of the protein.

SDS PAGE to determine purity of the protein.

LAL to determine quantity of endotoxin.

Note

This product is intended for research use only.

Summary

Research topic

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

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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