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Leptin, Recombinant, Mouse (Ob, Obese Protein, Obesity Factor)

Cat no: L1670-10A

Leptin, Recombinant, Mouse (Ob, Obese Protein, Obesity Factor)

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. \n\nRecombinant Murine Leptin is a single, non-glycosylated, polypeptide chain containing 147 amino acids and having a molecular mass of 16,240 Dalton. \n\nSequence:\nThe sequence of the first five N-terminal amino acids was determined and was found to be Met-Val-Pro-Ile-Gln. \n\nDimers and Aggregates:\n(same/less than) 1% as determined by silver-stained SDS-PAGE gel analysis. \n\nBiological Activity:\nRecombinant mouse Leptin is fully biologically active when compared to standards. Biological activity of Murine 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 5ug Leptin/gram body weight for a period of 14 days. Significant effects on body weight, food consumption, and plasma glucose levels were observed to saline-treated controls. \n\nProtein Content:\nProtein quantitation was carried out by two independent methods: \n1. UV spectroscopy at 280nm using the absorbency value of 0.201 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). \n2. Analysis by RP-HPLC, using a calibrated solution of Leptin as a Reference Standard.\n\nStorage and Stability:\nReconstitute to nominal volume by adding sterile dH2O and store at -20 degrees C. Reconstituted product is stable for 12 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

L1670-10A

Size

200ug

Form

Supplied as a lyophilized powder in 50mM NH4HCO3, pH 8.0. Reconstitute in sterile dH2O to a concentration > 0.1mg/ml. Can be further diluted to other aqueous solutions

Purity

(same/more than) 97% by RP-HPLC, FPLC, or reducing/non-reducing SDS-PAGE Silver Stain. Chromatographically purified. Endotoxin: (same/more than) 0.1ng/ug (IEU/ug)

References

1. Brief communication: Sleep curtailment in healthy young men is associated with decreased leptin levels, elevated ghrelin levels, and increased hunger and appetite. Spiegel K, Tasali E, Van Cauter E, Ann Intern Med 2004 Dec 7;141(11):846-50 2. Leptin reduces the development of the initial precancerous lesions induced by azoxymethane in the rat colonic mucosa. Stein DE, Kral JG, Gastroenterology 2004 Dec;127(6):1866-7; author reply 1867-8 3. [Leptin and beta-blockers in bone metabolism] Takeda S, Clin Calcium 2004 Feb;14(2):241-7 4. Plasma leptin and breast cancer risk: a prospective study in northern Sweden. Stattin P, Soderberg S, Lenner P, Breast Cancer Res Treat 2004 Aug;86(3):191-6 5. Recombinant human leptin in women with hypothalamic amenorrhea. LaMarca A, Volpe A, N Engl J Med 2004 Nov 25;351(22):2343; author reply 2343 6. The direct effect of leptin on skeletal muscle thermogenesis is mediated by substrate cycling between de novo lipogenesis and lipid oxidation. Solinas G, Summermatter S, Gubler M, Montani JP, FEBS Lett 2004 Nov 19;577(3):539-44.

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