Technical Data
Leptin (Ob, Obese Protein, Obesity Factor)
OB (or leptin) is a 16kD protein produced primarily in white adipose tissue, but also in brown fat and the placenta. It is first identified by positional cloning. It is involved in regulating the food intake, energy expenditure, whole-body energy balance in rodents and humans. In addition to its metabolic control role, OB also plays important roles in reproduction, immunological response and neuroendocrine signalling.

Suitable for use in Western Blot. Other applications not tested.

Recommended Dilution:
Western Blot: 1:2000
Optimal dilutions to be determined by the researcher.

Storage and Stability:
Lyophilized powder may be stored at 4C for short-term only. Reconstitute to nominal volume by adding sterile 40-50% glycerol and store at -20C. Reconstituted product is stable for 12 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
PabIgGAffinity Purified
200ug-20CBlue IceMouseRabbit
E. coli-expressed recombinant OB receptor, aa217-376
Purified by Protein A affinity chromatography.
Supplied as a lyophilized powder in 0.09% sodium azide.
Reacts with recombinant and natural mouse OB receptor.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Zhang, Y. et al. (1994) Positional cloning of the mouse obese gene and its human homologue. Nature 372:425-432 2. Pelleymounter, M.A. et al. (1995) Effects of the obese gene product on body weight regulation in ob/ob mice. Science 269:540543 3. Halaas, J.L. et al. (1995) Weight-reducing effects of the plasma protein encoded by the obese gene. Science 269:543-546 4. Campfield, L.A. et al. (1995) Recombinant mouse OB protein: evidence for a peripheral signal linking adiposity and central neural networks. Science 269:546-549 5. Saladin, R. et al. (1995) Transient increase in obese gene expression after food intake or insulin administration. Nature 377:527-529 6. Houseknecht, K.L. et al. (1998) The biology of leptin: a review. J Anim Sci 76(5):1405-1420.